Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1

Gene

hdrA1

Organism
Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Part of a complex that catalyzes the reversible reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme M) and H-S-CoB (coenzyme B). May act as the catalytic subunit (By similarity).By similarity

Catalytic activityi

Coenzyme B + coenzyme M + methanophenazine = N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + dihydromethanophenazine.

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterBy similarityNote: Binds 4 [4Fe-4S] clusters per subunit.By similarity
  • FADBy similarity

Pathwayi: coenzyme M-coenzyme B heterodisulfide reduction

This protein is involved in step 1 of the subpathway that synthesizes coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide.
Proteins known to be involved in this subpathway in this organism are:
  1. CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1 (hdrA1), CoB--CoM heterodisulfide reductase subunit B (hdrB), CoB--CoM heterodisulfide reductase iron-sulfur subunit C (hdrC), CoB--CoM heterodisulfide reductase iron-sulfur subunit A 2 (hdrA2)
This subpathway is part of the pathway coenzyme M-coenzyme B heterodisulfide reduction, which is itself part of Cofactor metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes coenzyme B and coenzyme M from coenzyme M-coenzyme B heterodisulfide, the pathway coenzyme M-coenzyme B heterodisulfide reduction and in Cofactor metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi249Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi252Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi255Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi259Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi296Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi299Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi302Iron-sulfur 2 (4Fe-4S)Sequence analysis1
Metal bindingi306Iron-sulfur 1 (4Fe-4S)Sequence analysis1
Metal bindingi593Iron-sulfur 3 (4Fe-4S)Sequence analysis1
Metal bindingi596Iron-sulfur 3 (4Fe-4S)Sequence analysis1
Metal bindingi599Iron-sulfur 3 (4Fe-4S)Sequence analysis1
Metal bindingi603Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi626Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi629Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi632Iron-sulfur 4 (4Fe-4S)Sequence analysis1
Metal bindingi636Iron-sulfur 3 (4Fe-4S)Sequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi153 – 176FADSequence analysisAdd BLAST24

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Methanogenesis

Keywords - Ligandi

4Fe-4S, FAD, Flavoprotein, Iron, Iron-sulfur, Metal-binding

Enzyme and pathway databases

UniPathwayiUPA00647; UER00700.

Names & Taxonomyi

Protein namesi
Recommended name:
CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1 (EC:1.8.98.1)
Gene namesi
Name:hdrA1
Synonyms:hdrA_1
Ordered Locus Names:MK0249
OrganismiMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938)
Taxonomic identifieri190192 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus
Proteomesi
  • UP000001826 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001500581 – 669CoB--CoM heterodisulfide reductase iron-sulfur subunit A 1Add BLAST669

Interactioni

Subunit structurei

The heterodisulfide reductase is composed of three subunits; HdrA, HdrB and HdrC.By similarity

Protein-protein interaction databases

STRINGi190192.MK0249.

Structurei

3D structure databases

ProteinModelPortaliQ8TYP4.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini239 – 2704Fe-4S ferredoxin-type 1PROSITE-ProRule annotationAdd BLAST32
Domaini287 – 3184Fe-4S ferredoxin-type 2PROSITE-ProRule annotationAdd BLAST32
Domaini584 – 6134Fe-4S ferredoxin-type 3PROSITE-ProRule annotationAdd BLAST30
Domaini617 – 6464Fe-4S ferredoxin-type 4PROSITE-ProRule annotationAdd BLAST30

Sequence similaritiesi

Belongs to the HdrA family.Curated
Contains 4 4Fe-4S ferredoxin-type domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG02235. Archaea.
COG1148. LUCA.
HOGENOMiHOG000230698.
KOiK03388.
OMAiCTPKIHE.

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
PF13187. Fer4_9. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8TYP4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGDKDDVRIG VFVCHCGVNI KASVDVEEVV EYAKKLPGVV YATDYPFFCA
60 70 80 90 100
DPGQEIIQEA IKEHDLDRVV VAACTPKIHE NTFRNCVKEA GLSPYYMEMV
110 120 130 140 150
NIREHCSFVH MQEPEKATEK AKDLIRAAVE RAKRLEDVPT KEVEVENSVL
160 170 180 190 200
IIGGGIAGIQ AALDLADQGF KVYLVEKEPT IGGNMARLAK TFPTDDCAMU
210 220 230 240 250
ILAPKMVQVG NHPNIEMITY AEVKDVDGYI GNFEVTIEKK PRYVDEDACT
260 270 280 290 300
GCGVCAEVCP IEVPNEFDLG IGTRKAIYVP FPQAMPLVYT IDMEHCIQCG
310 320 330 340 350
LCEEACPQDP PAIDFDQEPE EIRLKVGTII VATGYEEFDA SKLEEYGYGK
360 370 380 390 400
YDNVITTLEL ERMINPAGPT EGHVIRPSDG KEPHRIVFIH CVGSRCPGKE
410 420 430 440 450
EKGEAYCSRI CCMFILKNAQ LIKQHEPDAE VYCCYMDVRA FGKGYEEYYE
460 470 480 490 500
RAQKQFGVRF IRGRPAEIVE DPETKNLIVR VEDTLTGEPM EIEADLVVLG
510 520 530 540 550
CGLVAPEETY SKLADILGID RSPDGFFKEL HPKLEPVSTK VRGVQIAGVA
560 570 580 590 600
QGPKDIPDTV AQAKGAASEA SIPMSQGKVE IELITATVDE DVCGGCGACA
610 620 630 640 650
QVCPFDAIEM VEKDGKRVAE VQDVACQGCG QCAAACPSGA MQLRYYRDEQ
660
LMPQIEALLA EALEEEEEE
Length:669
Mass (Da):73,742
Last modified:February 26, 2008 - v3
Checksum:iC2D8D120157026E5
GO

Non-standard residue

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Non-standard residuei200SelenocysteineCurated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009439 Genomic DNA. Translation: AAM01466.1.

Genome annotation databases

EnsemblBacteriaiAAM01466; AAM01466; MK0249.
KEGGimka:MK0249.

Keywords - Coding sequence diversityi

Selenocysteine

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009439 Genomic DNA. Translation: AAM01466.1.

3D structure databases

ProteinModelPortaliQ8TYP4.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi190192.MK0249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAM01466; AAM01466; MK0249.
KEGGimka:MK0249.

Phylogenomic databases

eggNOGiarCOG02235. Archaea.
COG1148. LUCA.
HOGENOMiHOG000230698.
KOiK03388.
OMAiCTPKIHE.

Enzyme and pathway databases

UniPathwayiUPA00647; UER00700.

Family and domain databases

Gene3Di3.50.50.60. 4 hits.
InterProiIPR017896. 4Fe4S_Fe-S-bd.
IPR017900. 4Fe4S_Fe_S_CS.
IPR023753. FAD/NAD-binding_dom.
[Graphical view]
PfamiPF12838. Fer4_7. 1 hit.
PF13187. Fer4_9. 1 hit.
PF07992. Pyr_redox_2. 1 hit.
[Graphical view]
SUPFAMiSSF51905. SSF51905. 1 hit.
PROSITEiPS00198. 4FE4S_FER_1. 4 hits.
PS51379. 4FE4S_FER_2. 4 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHDRA1_METKA
AccessioniPrimary (citable) accession number: Q8TYP4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: February 26, 2008
Last modified: May 11, 2016
This is version 92 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.