GCDB_ACIFV
ID GCDB_ACIFV Reviewed; 375 AA.
AC Q9ZAA6; D2RM86;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Glutaconyl-CoA decarboxylase subunit beta;
DE EC=7.2.4.5;
DE AltName: Full=Carboxylyase;
GN Name=gcdB; OrderedLocusNames=Acfer_1834;
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], PROTEIN SEQUENCE OF 72-83 AND 233-243,
RP AND ALKYLATION.
RX PubMed=10027965; DOI=10.1046/j.1365-2958.1999.01189.x;
RA Braune A., Bendrat K., Rospert S., Buckel W.;
RT "The sodium ion translocating glutaconyl-CoA decarboxylase from
RT Acidaminococcus fermentans: cloning and function of the genes forming a
RT second operon.";
RL Mol. Microbiol. 31:473-487(1999).
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).
CC -!- FUNCTION: Tunnel subunit of the primary sodium pump glutaconyl-CoA
CC 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.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the GcdB/MmdB/OadB family. {ECO:0000305}.
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DR EMBL; AF030576; AAC69173.1; -; Genomic_DNA.
DR EMBL; CP001859; ADB48188.1; -; Genomic_DNA.
DR RefSeq; WP_012939171.1; NC_013740.1.
DR AlphaFoldDB; Q9ZAA6; -.
DR SMR; Q9ZAA6; -.
DR STRING; 591001.Acfer_1834; -.
DR TCDB; 3.B.1.1.3; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR PRIDE; Q9ZAA6; -.
DR EnsemblBacteria; ADB48188; ADB48188; Acfer_1834.
DR KEGG; afn:Acfer_1834; -.
DR eggNOG; COG1883; Bacteria.
DR HOGENOM; CLU_036168_0_0_9; -.
DR OMA; PMIADPK; -.
DR OrthoDB; 662061at2; -.
DR BioCyc; MetaCyc:MON-1055; -.
DR BRENDA; 7.2.4.5; 85.
DR SABIO-RK; Q9ZAA6; -.
DR UniPathway; UPA00533; UER00688.
DR Proteomes; UP000001902; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0018801; F:glutaconyl-CoA decarboxylase activity; IEA:UniProtKB-EC.
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; IPR005661; OadB_MmdB.
DR PANTHER; PTHR35806; PTHR35806; 1.
DR Pfam; PF03977; OAD_beta; 1.
DR PIRSF; PIRSF015658; MmdB_OadB; 1.
DR TIGRFAMs; TIGR01109; Na_pump_decarbB; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Decarboxylase; Direct protein sequencing; Ion transport;
KW Lyase; Membrane; Reference proteome; Sodium; Sodium transport; Translocase;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..375
FT /note="Glutaconyl-CoA decarboxylase subunit beta"
FT /id="PRO_0000218561"
FT TRANSMEM 16..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 46..65
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 74..96
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 107..130
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..232
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 254..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 316..332
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 345..369
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 375 AA; 38897 MW; 393D621373A75018 CRC64;
MDAFVVALTS VIQDSGFVAF TWGNAVMMLV GCILLYLAIV KGFEPLLLSP IAFGCILANV
PRTGFETDPG VMQLILGGIK YEIFPPLIFM GVGAMTDFGP LIANPKTLLL GAAAQIGVFV
ALLGAMLLGF NVKEASAIGI IGGADGPTSI YLASKMAPHL LGAIAVAAYS YMSLVPLIQP
PVMKLFTSKE ERKIKMAQLR TVTHFEKVVF PIVTTIFISL LLPSVCSLIG MLMLGNLFTE
SGCMDRLSDT AQNALMNSVT IMLATGTGLT MKAESFLTLQ TIEIICLGLV AFIGGTAGGV
LFGKLMSKLD GGKTNPLIGS AGVSAVPMAA RVSQVVGQQA DPGNFLLMHA MGPNVAGVIG
TAVAAGTMLA MVGGK
