GCDA_ACIFV
ID GCDA_ACIFV Reviewed; 587 AA.
AC Q06700; D2RM69;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Glutaconyl-CoA decarboxylase subunit alpha;
DE EC=7.2.4.5;
DE AltName: Full=Carboxyltransferase;
GN Name=gcdA; OrderedLocusNames=Acfer_1817;
OS Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS 106432 / VR4).
OC Bacteria; Firmicutes; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=591001;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX PubMed=8382157; DOI=10.1111/j.1432-1033.1993.tb17598.x;
RA Bendrat K., Buckel W.;
RT "Cloning, sequencing and expression of the gene encoding the
RT carboxytransferase subunit of the biotin-dependent Na+ pump glutaconyl-CoA
RT decarboxylase from Acidaminococcus fermentans in Escherichia coli.";
RL Eur. J. Biochem. 211:697-702(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4;
RX PubMed=21304687; DOI=10.4056/sigs.1002553;
RA Chang Y.J., Pukall R., Saunders E., Lapidus A., Copeland A., Nolan M.,
RA Glavina Del Rio T., Lucas S., Chen F., Tice H., Cheng J.F., Han C.,
RA Detter J.C., Bruce D., Goodwin L., Pitluck S., Mikhailova N., Liolios K.,
RA Pati A., Ivanova N., Mavromatis K., Chen A., Palaniappan K., Land M.,
RA Hauser L., Jeffries C.D., Brettin T., Rohde M., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Acidaminococcus fermentans type strain
RT (VR4).";
RL Stand. Genomic Sci. 3:1-14(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-587.
RX PubMed=8365476; DOI=10.1016/0014-5793(93)80247-r;
RA Bendrat K., Mueller U., Klees A.-G., Buckel W.;
RT "Identification of the gene encoding the activator of (R)-2-
RT hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans by gene
RT expression in Escherichia coli.";
RL FEBS Lett. 329:329-331(1993).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 548-587.
RX PubMed=7607244; DOI=10.1111/j.1432-1033.1995.0698h.x;
RA Mueller U., Buckel W.;
RT "Activation of (R)-2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus
RT fermentans.";
RL Eur. J. Biochem. 230:698-704(1995).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=12853465; DOI=10.1093/emboj/cdg358;
RA Wendt K.S., Schall I., Huber R., Buckel W., Jacob U.;
RT "Crystal structure of the carboxyltransferase subunit of the bacterial
RT sodium ion pump glutaconyl-coenzyme A decarboxylase.";
RL EMBO J. 22:3493-3502(2003).
CC -!- FUNCTION: Decarboxylase subunit of the primary sodium pump glutaconyl-
CC CoA decarboxylase (GCD).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-glutaconyl-CoA + H(+) + Na(+)(in) = (2E)-butenoyl-CoA +
CC CO2 + Na(+)(out); Xref=Rhea:RHEA:23972, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:29101, ChEBI:CHEBI:57332,
CC ChEBI:CHEBI:57353; EC=7.2.4.5;
CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
CC hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 5/5.
CC -!- SUBUNIT: Heterooctamer consisting of two alpha, two beta, two gamma and
CC two delta subunits.
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DR EMBL; X69435; CAA49210.1; -; Genomic_DNA.
DR EMBL; CP001859; ADB48171.1; -; Genomic_DNA.
DR EMBL; X59645; CAA42195.1; -; Genomic_DNA.
DR PIR; S29787; S29787.
DR RefSeq; WP_012939154.1; NC_013740.1.
DR PDB; 1PIX; X-ray; 2.20 A; A/B=1-587.
DR PDBsum; 1PIX; -.
DR AlphaFoldDB; Q06700; -.
DR SMR; Q06700; -.
DR STRING; 591001.Acfer_1817; -.
DR DrugBank; DB01942; Formic acid.
DR TCDB; 3.B.1.1.3; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR EnsemblBacteria; ADB48171; ADB48171; Acfer_1817.
DR KEGG; afn:Acfer_1817; -.
DR eggNOG; COG4799; Bacteria.
DR HOGENOM; CLU_033980_0_0_9; -.
DR OMA; SENILMV; -.
DR OrthoDB; 123223at2; -.
DR BioCyc; MetaCyc:MON-1054; -.
DR BRENDA; 7.2.4.5; 85.
DR SABIO-RK; Q06700; -.
DR UniPathway; UPA00533; UER00688.
DR EvolutionaryTrace; Q06700; -.
DR Proteomes; UP000001902; Chromosome.
DR GO; GO:0018801; F:glutaconyl-CoA decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0016874; F:ligase activity; IEA:InterPro.
DR GO; GO:0019552; P:glutamate catabolic process via 2-hydroxyglutarate; IEA:UniProtKB-UniPathway.
DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW.
DR InterPro; IPR034733; AcCoA_carboxyl.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR011762; COA_CT_N.
DR InterPro; IPR045190; MCCB/AccD1-like.
DR PANTHER; PTHR22855; PTHR22855; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR SUPFAM; SSF52096; SSF52096; 2.
DR PROSITE; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS50980; COA_CT_NTER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Biotin; Decarboxylase; Direct protein sequencing;
KW Ion transport; Lyase; Reference proteome; Sodium; Sodium transport;
KW Translocase; Transport.
FT CHAIN 1..587
FT /note="Glutaconyl-CoA decarboxylase subunit alpha"
FT /id="PRO_0000087438"
FT DOMAIN 31..298
FT /note="CoA carboxyltransferase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01136"
FT DOMAIN 295..558
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01137"
FT REGION 31..558
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01138"
FT HELIX 7..10
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 25..47
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 63..70
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 77..80
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 105..112
FT /evidence="ECO:0007829|PDB:1PIX"
FT TURN 114..119
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 125..139
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 143..147
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 161..163
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 169..179
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 184..188
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 195..201
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 202..209
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 213..216
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 233..244
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1PIX"
FT TURN 259..261
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 267..271
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 291..294
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 295..297
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 306..308
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 309..312
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 323..328
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 332..334
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 347..354
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 357..364
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 389..404
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 409..413
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 422..426
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 429..441
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 447..451
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 453..456
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:1PIX"
FT TURN 469..471
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 472..477
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 482..486
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 488..505
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 511..526
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 530..536
FT /evidence="ECO:0007829|PDB:1PIX"
FT STRAND 538..542
FT /evidence="ECO:0007829|PDB:1PIX"
FT TURN 545..547
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 548..559
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 569..571
FT /evidence="ECO:0007829|PDB:1PIX"
FT HELIX 574..583
FT /evidence="ECO:0007829|PDB:1PIX"
SQ SEQUENCE 587 AA; 64347 MW; BF1C0D2F2DCA86DA CRC64;
MGFYSMPRYF QNMPQVGKPL KKADAANEEQ LKKIEEEIHQ LIKEAQEAGK ADADVNKRGE
LTALQRIEKL VEPGSWRPLN TLFNPQGNKN GSVAIVKGLG RVNGKWCVVV ASDNKKLAGA
WVPGQAECLL RASDTAKTLH VPLVYVLNCS GVKFDEQEKV YPNRRGGGTP FFRNAELNQL
GIPVIVGIYG TNPAGGGYHS ISPTVIIAHE KANMAVGGAG IMGGMNPKGH VDLEYANEIA
DMVDRTGKTE PPGAVDIHYT ETGFMREVYA SEEGVLEGIK KYVGMLPKYD PEFFRVDDPK
APAFPADDLY SMVPLNDKRA YDIYNVIARL FDNSELHEYK KGYGPEMVTG LAKVNGLLVG
VVANVQGLLM NYPEYKAAGS VGIGGKLYRQ GLVKMNEFVT LCARDRLPIV WIQDTTGIDV
GNDAEKAELL GLGQSLIYSI QTSHIPQFEI TLRKGTAAAH YVLGGPQGND TNAFSIGTAA
TEIAVMNGET AATAMYSRRL AKDRKAGKDL QPTIDKMNNL IQAFYTKSRP KVCAELGLVD
EIVDMNKIRG YVEAFTEAAY QNPESICPFH QMILPRAIRE FETFVKK
