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Database: UniProt
Entry: Q9ZAA7
LinkDB: Q9ZAA7
Original site: Q9ZAA7 
ID   GCDC_ACIFV              Reviewed;         145 AA.
AC   Q9ZAA7; D2RM87;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   16-JAN-2019, entry version 96.
DE   RecName: Full=Glutaconyl-CoA decarboxylase subunit gamma;
DE            EC=4.1.1.70;
DE   AltName: Full=Biotin carrier;
GN   Name=gcdC; OrderedLocusNames=Acfer_1835;
OS   Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / VR4).
OC   Bacteria; Firmicutes; Negativicutes; Acidaminococcales;
OC   Acidaminococcaceae; Acidaminococcus.
OX   NCBI_TaxID=591001;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-34.
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
RT   a second operon.";
RL   Mol. Microbiol. 31:473-487(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25085 / DSM 20731 / 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.,
RA   Liolios K., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Brettin T.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   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: Biotin carrier subunit of the primary sodium pump
CC       glutaconyl-CoA decarboxylase (GCD).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(E)-glutaconyl-CoA + H(+) = (2E)-butenoyl-CoA + CO2;
CC         Xref=Rhea:RHEA:23972, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57332, ChEBI:CHEBI:57353; EC=4.1.1.70;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC   -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
CC       hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step
CC       5/5.
CC   -!- SUBUNIT: Heterooctamer consisting of two alpha, two beta, two
CC       gamma and two delta subunits.
DR   EMBL; AF030576; AAC69172.1; -; Genomic_DNA.
DR   EMBL; CP001859; ADB48189.1; -; Genomic_DNA.
DR   RefSeq; WP_012939172.1; NC_013740.1.
DR   ProteinModelPortal; Q9ZAA7; -.
DR   SMR; Q9ZAA7; -.
DR   STRING; 591001.Acfer_1835; -.
DR   TCDB; 3.B.1.1.3; the na(+)-transporting carboxylic acid decarboxylase (nat-dc) family.
DR   EnsemblBacteria; ADB48189; ADB48189; Acfer_1835.
DR   KEGG; afn:Acfer_1835; -.
DR   eggNOG; ENOG4105PV1; Bacteria.
DR   eggNOG; COG0511; LUCA.
DR   HOGENOM; HOG000008877; -.
DR   OMA; DQVTENQ; -.
DR   OrthoDB; 1938042at2; -.
DR   BioCyc; AFER591001:G1GH7-1898-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-1056; -.
DR   SABIO-RK; Q9ZAA7; -.
DR   UniPathway; UPA00533; UER00688.
DR   Proteomes; UP000001902; Chromosome.
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; IPR001882; Biotin_BS.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   1: Evidence at protein level;
KW   Biotin; Complete proteome; Decarboxylase; Direct protein sequencing;
KW   Ion transport; Lyase; Reference proteome; Sodium; Sodium transport;
KW   Transport.
FT   CHAIN         1    145       Glutaconyl-CoA decarboxylase subunit
FT                                gamma.
FT                                /FTId=PRO_0000146839.
FT   DOMAIN       77    145       Biotinyl-binding. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01066}.
FT   COMPBIAS     23     75       Ala-rich.
FT   MOD_RES     112    112       N6-biotinyllysine. {ECO:0000250,
FT                                ECO:0000255|PROSITE-ProRule:PRU01066}.
SQ   SEQUENCE   145 AA;  13908 MW;  4546006D4F2F4C6B CRC64;
     MRKFNVNVNG TVYTVEVEEV GGAVTAAPAA PAAPAAAPAA APVAAAPAAA PAPAPAAAPA
     AAPAPAAKPA AAAPAGSVTV SAPMPGKILS VNVKPGDKVE AGDVLLILEA MKMQNEIMAP
     EDGTVSEVRV NAGDTVATGD VMVIL
//
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