GCTA_ACIFV
ID GCTA_ACIFV Reviewed; 320 AA.
AC Q59111; D2RM71;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Glutaconate CoA-transferase subunit A;
DE EC=2.8.3.12;
DE AltName: Full=GCT large subunit;
GN Name=gctA; OrderedLocusNames=Acfer_1819;
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 PROTEIN SEQUENCE OF 2-13.
RX PubMed=7957258; DOI=10.1111/j.1432-1033.1994.tb20024.x;
RA Mack M., Bendrat K., Zelder O., Eckel E., Linder D., Buckel W.;
RT "Location of the two genes encoding glutaconate coenzyme A-transferase at
RT the beginning of the hydroxyglutarate operon in Acidaminococcus
RT fermentans.";
RL Eur. J. Biochem. 226:41-51(1994).
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 X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS).
RX PubMed=9083111; DOI=10.1016/s0969-2126(97)00198-6;
RA Jacob U., Mack M., Clausen T., Huber R., Buckel W., Messerschmidt A.;
RT "Glutaconate CoA-transferase from Acidaminococcus fermentans: the crystal
RT structure reveals homology with other CoA-transferases.";
RL Structure 5:415-426(1997).
CC -!- FUNCTION: Catalyzes the transfer of the CoA moiety from acetyl-CoA to
CC (R)-2-hydroxyglutarate and related compounds like glutaconate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetyl-CoA + trans-glutaconate = (2E)-glutaconyl-CoA +
CC acetate; Xref=Rhea:RHEA:23208, ChEBI:CHEBI:30089, ChEBI:CHEBI:36460,
CC ChEBI:CHEBI:57288, ChEBI:CHEBI:57353; EC=2.8.3.12;
CC -!- PATHWAY: Amino-acid degradation; L-glutamate degradation via
CC hydroxyglutarate pathway; crotonoyl-CoA from L-glutamate: step 3/5.
CC -!- SUBUNIT: Heterooctamer of four A and four B subunits.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the 3-oxoacid CoA-transferase subunit A family.
CC {ECO:0000305}.
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DR EMBL; X81440; CAA57199.1; -; Genomic_DNA.
DR EMBL; CP001859; ADB48173.1; -; Genomic_DNA.
DR PIR; S51051; S51051.
DR RefSeq; WP_012939156.1; NC_013740.1.
DR PDB; 1POI; X-ray; 2.50 A; A/C=2-318.
DR PDBsum; 1POI; -.
DR AlphaFoldDB; Q59111; -.
DR SMR; Q59111; -.
DR DIP; DIP-6200N; -.
DR IntAct; Q59111; 1.
DR STRING; 591001.Acfer_1819; -.
DR EnsemblBacteria; ADB48173; ADB48173; Acfer_1819.
DR KEGG; afn:Acfer_1819; -.
DR eggNOG; COG1788; Bacteria.
DR HOGENOM; CLU_049557_0_0_9; -.
DR OMA; WGPRRKP; -.
DR OrthoDB; 1660857at2; -.
DR BioCyc; MetaCyc:MON-1028; -.
DR BRENDA; 2.8.3.12; 85.
DR SABIO-RK; Q59111; -.
DR UniPathway; UPA00533; UER00686.
DR EvolutionaryTrace; Q59111; -.
DR Proteomes; UP000001902; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0018730; F:glutaconate CoA-transferase activity; IEA:UniProtKB-EC.
DR GO; GO:0019552; P:glutamate catabolic process via 2-hydroxyglutarate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004165; CoA_trans_fam_I.
DR InterPro; IPR037171; NagB/RpiA_transferase-like.
DR Pfam; PF01144; CoA_trans; 1.
DR SMART; SM00882; CoA_trans; 1.
DR SUPFAM; SSF100950; SSF100950; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Reference proteome;
KW Transferase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7957258"
FT CHAIN 2..320
FT /note="Glutaconate CoA-transferase subunit A"
FT /id="PRO_0000157927"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 20..23
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 33..41
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 67..75
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 78..80
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 85..93
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 96..100
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 103..115
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 118..123
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 129..132
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 138..142
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 160..169
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 174..183
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 198..204
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 205..215
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 225..227
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 237..240
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 242..247
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 251..253
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 258..267
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 271..281
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 282..284
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 288..295
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 297..301
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 307..309
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 315..317
FT /evidence="ECO:0007829|PDB:1POI"
SQ SEQUENCE 320 AA; 35722 MW; C51B214FE17FEB46 CRC64;
MSKVMTLKDA IAKYVHSGDH IALGGFTTDR KPYAAVFEIL RQGITDLTGL GGAAGGDWDM
LIGNGRVKAY INCYTANSGV TNVSRRFRKW FEAGKLTMED YSQDVIYMMW HAAALGLPFL
PVTLMQGSGL TDEWGISKEV RKTLDKVPDD KFKYIDNPFK PGEKVVAVPV PQVDVAIIHA
QQASPDGTVR IWGGKFQDVD IAEAAKYTIV TCEEIISDEE IRRDPTKNDI PGMCVDAVVL
APYGAHPSQC YGLYDYDNPF LKVYDKVSKT QEDFDAFCKE WVFDLKDHDE YLNKLGATRL
INLKVVPGLG YHIDMTKEDK
