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Protein

Acetyl-CoA decarbonylase/synthase complex subunit alpha 1

Gene

cdhA1

Organism
Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Part of the ACDS complex that catalyzes the reversible cleavage of acetyl-CoA, allowing growth on acetate as sole source of carbon and energy. The alpha-epsilon subcomponent functions as a carbon monoxide dehydrogenase.UniRule annotation

Catalytic activityi

CO + H2O + 2 oxidized ferredoxin = CO2 + 2 reduced ferredoxin + 2 H+.UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • [4Fe-4S] clusterUniRule annotationNote: Binds 7 [4Fe-4S] clusters per heterotetramer.UniRule annotation
  • [Ni-4Fe-4S] clusterUniRule annotationNote: Binds 2 [Ni-4Fe-4S] clusters per heterotetramer.UniRule annotation

pH dependencei

Optimum pH is 8-9.

Pathwayi: methanogenesis from acetate

This protein is involved in the pathway methanogenesis from acetate, which is part of One-carbon metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway methanogenesis from acetate and in One-carbon metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi73Iron-sulfur 1 (4Fe-4S); shared with dimeric partnerUniRule annotation1
Metal bindingi76Iron-sulfur 2 (4Fe-4S)UniRule annotation1
Metal bindingi77Iron-sulfur 1 (4Fe-4S); shared with dimeric partnerUniRule annotation1
Metal bindingi79Iron-sulfur 2 (4Fe-4S)UniRule annotation1
Metal bindingi84Iron-sulfur 2 (4Fe-4S)UniRule annotation1
Metal bindingi94Iron-sulfur 2 (4Fe-4S)UniRule annotation1
Binding sitei117Carbon monoxide; via tele nitrogenUniRule annotation1
Metal bindingi250Nickel-iron-sulfur (Ni-4Fe-4S); via tele nitrogenUniRule annotation1
Metal bindingi278Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation1
Metal bindingi323Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation1
Metal bindingi417Iron-sulfur 3 (4Fe-4S)UniRule annotation1
Metal bindingi420Iron-sulfur 3 (4Fe-4S)UniRule annotation1
Metal bindingi423Iron-sulfur 3 (4Fe-4S)UniRule annotation1
Metal bindingi427Iron-sulfur 4 (4Fe-4S)UniRule annotation1
Metal bindingi455Iron-sulfur 4 (4Fe-4S)UniRule annotation1
Metal bindingi458Iron-sulfur 4 (4Fe-4S)UniRule annotation1
Metal bindingi461Iron-sulfur 4 (4Fe-4S)UniRule annotation1
Metal bindingi465Iron-sulfur 3 (4Fe-4S)UniRule annotation1
Metal bindingi523Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation1
Metal bindingi552Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation1
Metal bindingi587Nickel-iron-sulfur (Ni-4Fe-4S)UniRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processMethanogenesis
Ligand4Fe-4S, Iron, Iron-sulfur, Metal-binding, Nickel

Enzyme and pathway databases

UniPathwayiUPA00642

Names & Taxonomyi

Protein namesi
Recommended name:
Acetyl-CoA decarbonylase/synthase complex subunit alpha 1UniRule annotation (EC:1.2.7.4UniRule annotation)
Short name:
ACDS complex subunit alpha 1UniRule annotation
Alternative name(s):
ACDS complex carbon monoxide dehydrogenase subunit alpha 1UniRule annotation
Short name:
ACDS CODH subunit alpha 1UniRule annotation
Gene namesi
Name:cdhA1UniRule annotation
Ordered Locus Names:MM_2089
OrganismiMethanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88) (Methanosarcina frisia)
Taxonomic identifieri192952 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanomicrobiaMethanosarcinalesMethanosarcinaceaeMethanosarcina
Proteomesi
  • UP000000595 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001550802 – 806Acetyl-CoA decarbonylase/synthase complex subunit alpha 1Add BLAST805

Proteomic databases

PRIDEiQ49161

Interactioni

Subunit structurei

Heterotetramer of two alpha and two epsilon subunits. The ACDS complex is made up of alpha, epsilon, beta, gamma and delta subunits with a probable stoichiometry of (alpha2epsilon2)4-beta8-(gamma1delta1)8.UniRule annotation

Protein-protein interaction databases

STRINGi192952.MM_2089

Structurei

3D structure databases

ProteinModelPortaliQ49161
SMRiQ49161
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini406 – 4364Fe-4S ferredoxin-type 1UniRule annotationAdd BLAST31
Domaini445 – 4754Fe-4S ferredoxin-type 2UniRule annotationAdd BLAST31

Domaini

Cluster B is an all-cysteinyl-liganded 4Fe-4S cluster; cluster C is a mixed Ni-Fe-S cluster which is the active site of CO oxidation. Cluster D is also an all-cysteinyl-liganded 4Fe-4S cluster that bridges the two subunits of the CODH dimer. Contains two additional 4Fe-4S clusters, dubbed E and F, that probably transport electrons from ferredoxin to the B cluster.UniRule annotation

Sequence similaritiesi

Belongs to the Ni-containing carbon monoxide dehydrogenase family.UniRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiarCOG02428 Archaea
COG1152 LUCA
HOGENOMiHOG000224351
KOiK00192
OMAiRNEREIP
OrthoDBiPOG093Z0139

Family and domain databases

Gene3Di1.10.1060.10, 1 hit
3.40.50.2030, 4 hits
HAMAPiMF_01137 CdhA, 1 hit
InterProiView protein in InterPro
IPR017896 4Fe4S_Fe-S-bd
IPR017900 4Fe4S_Fe_S_CS
IPR004460 CDHA
IPR004137 HCP/CODH
IPR009051 Helical_ferredxn
IPR016099 Prismane-like_a/b-sand
IPR011254 Prismane-like_sf
PANTHERiPTHR30109 PTHR30109, 1 hit
PfamiView protein in Pfam
PF03063 Prismane, 2 hits
SUPFAMiSSF46548 SSF46548, 1 hit
SSF56821 SSF56821, 1 hit
TIGRFAMsiTIGR00314 cdhA, 1 hit
PROSITEiView protein in PROSITE
PS00198 4FE4S_FER_1, 1 hit
PS51379 4FE4S_FER_2, 2 hits

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q49161-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKLTTGSFS IEDLESVQIT INNIVGAAKE AAEEKTKELG HMGPTPFPGL
60 70 80 90 100
ETYRDDWNLK LLDRYEPVVT PMCDQCCYCT YGPCDLSNNK RGACGIDMLG
110 120 130 140 150
HNGREFFLRV ITGTACHAAH GRHLLDHLIE VFGEELPLNL GQSDVLTPNI
160 170 180 190 200
TITTGQRPQT LGEIKPAMEH VEEQLTQLLA TVHAGQESAE IDYDSKALFS
210 220 230 240 250
GSLDHVGMEI SDIVQIAALD FPKADPEAPL IEMGMGTIDK DKPFLCVIGH
260 270 280 290 300
NVGGVTYMMD YMEEHELTDK VELGGLCCTA IDLTRYKEAD RRPPYTKVVG
310 320 330 340 350
SMSKELKIIR SGMPDVIVVD EQCVRGDIVP EAQKLKIPVI ASNAKIMYGL
360 370 380 390 400
PNRTDAGVEE TIEELKSGAI PGAVILDYEK LGEISVRLAQ EMHPIREAAG
410 420 430 440 450
VREIPSDEQL KEWVDKCADC GACYLACPIE LDIPEAMKFA KQGDFSYLED
460 470 480 490 500
LHDACIGCRR CEQVCKKEIP ILSVIEKASQ KIIAEEKGWM RAGRGQVSDA
510 520 530 540 550
EIRAEGLNLV MGTTPGIIAI IGCPNYSDCA KAVYYIAEEF LKRNYIVVGT
560 570 580 590 600
GCGSMDMGMY KDEDGKTLYE RFPGGFQSGG LVNIGSCVSN AHITGAAQKV
610 620 630 640 650
AGIFGGRTME GNLAEIADYV LNRVGACGLA WGAFSQKASS IGTGCNIYGI
660 670 680 690 700
PAVLGAHSSK YRRALIAKNY DESKWKVYDA RNGEEMPIPP APEFLLTTAE
710 720 730 740 750
TWQEAIPMMA KACLRPSDNS LGRSIKLTHW MELHDKYIGG LPEDWWKFIR
760 770 780 790 800
TEADLPLAKR ADLMKKLEAE RGWEIDWKKK KIISGPKIKF DVSAQPTNLK

RLCKGA
Length:806
Mass (Da):88,583
Last modified:January 23, 2007 - v3
Checksum:i8A6EE054FBE778AF
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L26487 Genomic DNA Translation: AAC37044.1
AE008384 Genomic DNA Translation: AAM31785.1
RefSeqiWP_011034020.1, NC_003901.1

Genome annotation databases

EnsemblBacteriaiAAM31785; AAM31785; MM_2089
GeneIDi24840339
KEGGimma:MM_2089
PATRICifig|192952.21.peg.2398

Similar proteinsi

Entry informationi

Entry nameiACDA1_METMA
AccessioniPrimary (citable) accession number: Q49161
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 122 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

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