Rv3577 Resolved · high

H37Rv Rv3577 · MTBC0 - · 288 aa · 4019262–4020128 (+) · RefSeq NP_218094.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)hypothetical protein
MTBC0 PGAP re-annotation
Revised (this work)Binuclear metallo-beta-lactamase (MBL)-fold metallo-hydrolase of the UPF0173/UlaG family (InterPro IPR050114), substrate unassigned. RefSeq leaves it 'hypothetical protein'. The MBL HxHxDH motif (His74-His76-Asp78-His79) was confirmed as a genuine two-metal centre by co-folding the chain with two metal ions on AlphaFold Server (independent Zn and Fe jobs, top model iPTM 0.98): the ions bind a single bridged binuclear site 3.2-3.4 A apart, partitioned into a three-histidine metal (His74/His76/His137) and an aspartate-plus-two-histidine metal (Asp78/His79/His235), with identical geometry for Zn or Fe. HHpred top hits (>=99.8%) are UPF0173/UlaG metal-dependent hydrolases (UlaG 2wyl; COG2220). The fold-paralogue safeguard withholds the RNase Z (held by Rv2407) and glyoxalase II (Rv0634c/Rv2581c) labels: only the fold-level family is claimed. The six metal ligands are effectively invariant across ~250,724 genomes (most frequent non-synonymous ligand variant 0.0032%). A structural prediction, not a biochemical assay.

Annotated on the H37Rv protein: this gene has no 1:1 ancestral MTBC0 anchor (PE/PPE, paralogue, IS element, or otherwise unanchored CDS).

Curated reference (UniProt)

UniProt P96859 TrEMBL · unreviewed · Predicted
UniProt nameMBL fold metallo-hydrolase

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category S Function unknown
eggNOG descriptionZn-dependent hydrolases of the beta-lactamase fold
Orthologous groupCOG2220

Orthology-based transfer (eggNOG 5.0.2, diamond). EC/KO/GO/CAZy are computed annotations, not manual curation; cross-check against the primary literature before treating a specific reaction as established.

Conservation & selection (intra-MTBC, 145 209 strains)

pN/pS 0.551 · relaxed/neutral
Polymorphic sites (≥ 0.1% of strains) 2 synonymous, 3 missense, 0 nonsense, 2 frameshift
Disruption 2 distinct premature-stop/frameshift site(s); most common in 0.57% of strains (821) · clonal

pN/pS from segregating SNPs (singletons removed) normalised by possible sites. Low pN/pS = purifying selection (a strong signal that a "hypothetical" is a real, constrained gene). A high pN/pS is ambiguous: relaxed constraint or positive selection (drug resistance, antigenic variation) inflate it; e.g. rpoB/katG/pncA score high here for resistance, not loss of function. A clonal disruption (one allele over a clade) suggests lineage pseudogenisation; a convergent one (many independent alleles) is typical of resistance loss-of-function.

Domains (Pfam, hmmscan --cut_ga)

No Pfam-A domain above the gathering threshold (or not yet scanned).

Structural neighbours (Foldseek on the ESMFold model, exploratory)

ESMFold model confidence: mean pLDDT 97.1 (very high). A confident model makes the fold comparison meaningful.

Best matches against the PDB, ranked by Foldseek homology probability. A high probability / TM-score suggests a shared fold; unless flagged sig (E < 0.01) these are fold hypotheses, not assignments.

TargetProbTME-valueDescription
3bv6-assembly1_C 1.00 0.61 9.6e-13 sig 3bv6-assembly1_C Crystal structure of uncharacterized metallo protein from Vibrio cholerae with beta-lactamase like fold
3x2y-assembly1_C 1.00 0.71 2.9e-11 sig 3x2y-assembly1_C Crystal structure of metallo-beta-lactamase H8A from Thermotoga maritima
3x2z-assembly1_C 1.00 0.72 6.7e-11 sig 3x2z-assembly1_C Crystal structure of metallo-beta-lactamase in complex with nickel from Thermotoga maritima
2wyl-assembly1_B 1.00 0.64 3.5e-11 sig 2wyl-assembly1_B Apo structure of a metallo-b-lactamase
3x2x-assembly1_C 1.00 0.70 5.6e-11 sig 3x2x-assembly1_C Crystal structure of metallo-beta-lactamase H48A from Thermotoga maritima
2wyl-assembly1_C 1.00 0.61 1.3e-11 sig 2wyl-assembly1_C Apo structure of a metallo-b-lactamase
2wyl-assembly1_F 1.00 0.63 2.3e-11 sig 2wyl-assembly1_F Apo structure of a metallo-b-lactamase
2wyl-assembly1_A 1.00 0.63 2.7e-11 sig 2wyl-assembly1_A Apo structure of a metallo-b-lactamase

Functional interaction network (STRING v12, guilt-by-association)

Closest characterised functional partner: arsB2 (arsenic transport integral membrane protein ArsB), high confidence from genomic context alone (score 875 excluding text-mining). This association is the citable seed of a function hypothesis for this hypothetical protein.

PartnerProductScoreNo text-miningChannels (≥400)
Rv3578 arsB2 arsenic transport integral membrane protein ArsB 875 875 ctx neighborhood:867
Rv3576 lppH lipoprotein LppH 746 746 ctx neighborhood:738
Rv3575c LacI family transcriptional regulator 676 676 ctx neighborhood:674
Rv1874 hyp hypothetical protein 645 645 ctx cooccurence:645
Rv0138 hyp hypothetical protein 542 543 ctx cooccurence:540
Rv2015c hyp hypothetical protein 538 538 ctx cooccurence:537
Rv2574 hyp hypothetical protein 513 513 ctx cooccurence:510
Rv0941c hyp hypothetical protein 512 512 ctx cooccurence:509
Rv1765c hyp hypothetical protein 511 512 ctx cooccurence:509
Rv3169 hyp hypothetical protein 496 496 ctx cooccurence:496
Rv1976c hyp hypothetical protein 468 469 ctx cooccurence:467
Rv1401 membrane protein 457 457 ctx cooccurence:454
Rv0272c hyp hypothetical protein 440 440 ctx cooccurence:436
Rv0293c hyp hypothetical protein 425 425 ctx cooccurence:418
Rv2721c hyp hypothetical protein 412 412 ctx cooccurence:409

STRING combines evidence channels (neighborhood, fusion, cooccurrence, coexpression, experimental, database, text-mining) into a 0–1000 score. The ctx badge marks edges carried by the genomic-context channels (conserved neighborhood, fusion, phylogenetic co-occurrence), which are independent of orthology and structure and the strongest signal for an unknown gene. The no text-mining column recomputes the score from data alone, so a link that does not depend on the literature is visible. Association is a function hypothesis, not proof: corroborate with the operon context and the primary literature before assigning a function.

Evidence

  • RefSeq: hypothetical protein; eggNOG COG2220 (Zn-dependent beta-lactamase-fold hydrolases)
  • MBL motif HxHxDH (His74/His76/Asp78/His79); Foldseek 3bv6 / 2wyl (prob 1.00)
  • AlphaFold Server metal co-folding (Zn + Fe): bridged binuclear site 3.2-3.4 A; ligands His74/His76/His137 + Asp78/His79/His235; iPTM 0.98
  • HHpred >=99.8%: UPF0173/UlaG metal-dependent hydrolases (UlaG 2wyl, COG2220)
  • Fold-paralogue safeguard: RNase Z (Rv2407) and glyoxalase II (Rv0634c/Rv2581c) labels withheld
  • Six metal-ligand codons effectively invariant across ~250,724 genomes (most frequent NS 0.0032%)
  • Curated against the companion dark-enzymes re-annotation (Guyeux 2026)

Sources

  • Ancestral sequence & coordinates: Harrison LB et al. (2024), An imputed ancestral reference genome for the MTBC, doi:10.1101/2023.09.07.556366
  • Product annotation: NCBI PGAP on MTBC0; legacy from H37Rv NC_000962.3 (RefSeq NP_218094.1)
  • Domains: Pfam-A via hmmscan --cut_ga — none above threshold
  • Sequence-level signal: ESM Atlas (EvolutionaryScale × BioHub) — exploratory
  • Controlled vocabulary: eggNOG-mapper 2.1.12 (Cantalapiedra et al. 2021, doi:10.1093/molbev/msab293), eggNOG 5.0 DB (Huerta-Cepas et al. 2019) — OG COG2220
  • Curated reference: UniProt P96859 (TrEMBL, unreviewed; Predicted)
  • Intra-MTBC selection: pN/pS and disruption from SPDI variants of 145 209 MTBC strains (this work, local collection vs H37Rv NC_000962.3)
  • Model confidence: ESMFold per-residue pLDDT (mean 97.1, very high)
  • Interaction network: STRING v12.0 (Szklarczyk et al. 2023, doi:10.1093/nar/gkac1000), taxon 83332, CC-BY 4.0 — 17 functional partner(s); context anchor arsB2
  • Primary literature: Guyeux C (2026). Structure-guided functional hypotheses for uncharacterised enzymes of Mycobacterium tuberculosis in preparation. doi:10.5281/zenodo.20571950

Ancestral MTBC0 protein sequence

>H37Rv|Rv3577|
MPTARSDAPLSVTWMGVATLLVDDGSSALMTDGYFSRPGLARVAAGKVSPSAERVDGCLARANVSRLTAVIPVHTHIDHAMDSALVADRTGAQLVGGESAANVGRGYGLPEESLVVAVPGEPIQLGAFDVTLVESHHCPPDRFPGVISAPLTPPVKASAYRCGEAWSTLVHHRPSGRRLLIQDSAGFVSGALAGYRADAAYLSVGQLGLQPPSYLLEYWTETVRTVGVRRVILIHWDDFFRPLSKPLRALPYAADDLDLSIRILDELAAQDGVALQMPTVWRREDPWM