Rv0338c Resolved · high auto-curated

H37Rv Rv0338c · MTBC0 mtbc0_000358 · 882 aa · 406516–409164 (-) · RefSeq NP_214852.1

Annotation: from legacy to revised

Legacy (H37Rv / Mycobrowser)iron-sulfur-binding reductase
MTBC0 PGAP re-annotationheterodisulfide reductase-related iron-sulfur binding cluster
Revised (this work)Heterodisulfide reductase-related iron-sulfur binding cluster. Pfam: Fer4_10 (PF13237.12), Fer4_9 (PF13187.12), CCG (PF02754.22).

Auto-curated: this verdict and function were generated by rules from PGAP + Pfam + Foldseek and have not been hand-reviewed.

Curated reference (UniProt)

UniProt O33268 TrEMBL · unreviewed · Evidence at protein level
UniProt nameProbable iron-sulfur-binding reductase

Functional vocabulary (eggNOG-mapper, orthology transfer)

COG category C Energy production and conversion
eggNOG descriptionFe-S oxidoreductase
Orthologous groupCOG0247

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 0.185 · strong purifying
Polymorphic sites (≥ 0.1% of strains) 25 synonymous, 14 missense, 0 nonsense, 0 frameshift

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)

PfamAccessioni-EvalueResiduesDescription
Fer4_10PF13237.12 1.6e-07290–403 4Fe-4S dicluster domain
Fer4_9PF13187.12 1.1e-10295–405 4Fe-4S dicluster domain
CCGPF02754.22 2.9e-19607–693 Cysteine-rich domain

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

Closest characterised functional partner: aspC (aspartate aminotransferase), high confidence from genomic context alone (score 719 excluding text-mining).

PartnerProductScoreNo text-miningChannels (≥400)
Rv3464 rmlB dTDP-glucose 4,6-dehydratase 811 812 coexpression:812
Rv1436 gap glyceraldehyde 3-phosphate dehydrogenase 748 733 coexpression:732
Rv0337c aspC aspartate aminotransferase 719 719 ctx neighborhood:695
Rv0632c echA3 enoyl-CoA hydratase EchA3 715 705 coexpression:695
Rv3029c fixA electron transfer flavoprotein subunit beta 837 585 textmining:625
Rv3028c fixB electron transfer flavoprotein subunit alpha 786 581 textmining:512
Rv2841c nusA transcription termination/antitermination protein NusA 554 555 coexpression:497
Rv3859c gltB glutamate synthase large subunit 602 552 ctx neighborhood:544
Rv0339c iniR transcriptional regulator 542 543 ctx neighborhood:532
Rv2783c gpsI bifunctional guanosine pentaphosphate synthetase/polyribonucleotide nucleotidyltransferase 527 508 coexpression:446
Rv2538c aroB 3-dehydroquinate synthase 515 491 coexpression:433
Rv0487 hyp hypothetical protein 453 453 ctx cooccurence:445
Rv1292 argS arginine--tRNA ligase 479 446
Rv3302c glpD2 glycerol-3-phosphate dehydrogenase 497 440 coexpression:407
Rv0244c fadE5 acyl-CoA dehydrogenase FadE5 460 439

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

  • Legacy H37Rv annotation: iron-sulfur-binding reductase
  • MTBC0 PGAP product: heterodisulfide reductase-related iron-sulfur binding cluster
  • Pfam (hmmscan --cut_ga): Fer4_10 PF13237.12 (E=2e-07), Fer4_9 PF13187.12 (E=1e-10), CCG PF02754.22 (E=3e-19)
  • (auto-curated by rules from PGAP + Pfam + Foldseek; not hand-reviewed)

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_214852.1)
  • Domains: Pfam-A via hmmscan --cut_ga — Fer4_10 (PF13237.12), Fer4_9 (PF13187.12), CCG (PF02754.22)
  • 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 COG0247
  • Curated reference: UniProt O33268 (TrEMBL, unreviewed; Evidence at protein level)
  • Intra-MTBC selection: pN/pS and disruption from SPDI variants of 145 209 MTBC strains (this work, local collection vs H37Rv NC_000962.3)
  • Interaction network: STRING v12.0 (Szklarczyk et al. 2023, doi:10.1093/nar/gkac1000), taxon 83332, CC-BY 4.0 — 44 functional partner(s); context anchor aspC
  • Primary literature: none located yet; annotation rests on the domain/homology sources above.

Ancestral MTBC0 protein sequence

>mtbc0_000358|Rv0338c|
MTTQTLIRLILGMSMTAVVGVFALRRVWWLYKLVMSGQPASGRTDNLGTRIWTQISEVLGQRRLLKWSIPGLAHFFTMWGFFILLTVYIEAYGLLFEERFHIPVIGRWDALGFLQDFFATAVFLGITTFAIIRILRNPREIGRSSRFYGSHNGGAWLVLLMIFNVIWTYVLVRGSAVNNGTLPYGNGAFLSQLFGAILRPLGQPANEIIETTALLLHIGVMLAFLILVLHSKHLHIFLAPINVTFKRLPDGLGPLLPLEADGKPIDFENPSEDAVFGRGKIEDFTWKGMLDFATCTECGRCQSQCPAWNTGKPLSPKLVIMDLRDHWMAKAPYILGQKDASAGGEAGHQEHHHVPESGFGRVPGHGPEQATRPLVGTEEQGGVIDPDVLWSCVTCGACVEQCPVDIEHVDHIVDMRRYQVMMESEFPSELSVLFKNLETKGNPWGQNASDRTNWIDEVDFDVPVYGQDVDSFDGYEYLFWVGCAGAYDDKAKKTTKAVAELLAVAGVKYLVLGAGETCNGDSARRSGNEFLFQQLAQQAVETLDGLFEGVETVDRKIVVTCPHCFNTIGKEYRQLGANYTVLHHTQLLNRLVRDKRLVPVTPVSQDITYHDPCYLGRHNKVYEAPRELIGAAGASLTEMPRHADRSFCCGAGGARMWMEEHIGKRINHERVDEALATDATAIATACPFCRVMVTDGVNDRQEEAGRSGVEVLDVAQVLLGSLDHDKAQLPAKGTAAKQAQERAPKAAPKAAAPVTPVEAPAEAPQAPAPAAPAAPVKGLGMAAGAKRPGAKKAAPTPAAPAAPAAPVKGLGIAAGAKRPGAKKTPPPAPGLAEPAAQPQPEAKPQPEPAAPPKPQTDGDPAAPAAPVKGLGIARGARPPGKR