GCTB_ACIFV
ID GCTB_ACIFV Reviewed; 266 AA.
AC Q59112; D2RM70;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Glutaconate CoA-transferase subunit B;
DE EC=2.8.3.12;
DE AltName: Full=GCT small subunit;
GN Name=gctB; OrderedLocusNames=Acfer_1818;
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 2-19 AND 44-66.
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 B family.
CC {ECO:0000305}.
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DR EMBL; X81440; CAA57200.1; -; Genomic_DNA.
DR EMBL; CP001859; ADB48172.1; -; Genomic_DNA.
DR PIR; S51052; S51052.
DR RefSeq; WP_012939155.1; NC_013740.1.
DR PDB; 1POI; X-ray; 2.50 A; B/D=3-262.
DR PDBsum; 1POI; -.
DR AlphaFoldDB; Q59112; -.
DR SMR; Q59112; -.
DR DIP; DIP-6201N; -.
DR IntAct; Q59112; 1.
DR STRING; 591001.Acfer_1818; -.
DR EnsemblBacteria; ADB48172; ADB48172; Acfer_1818.
DR KEGG; afn:Acfer_1818; -.
DR eggNOG; COG2057; Bacteria.
DR HOGENOM; CLU_069088_0_0_9; -.
DR OMA; YWVGNHS; -.
DR OrthoDB; 1380130at2; -.
DR BioCyc; MetaCyc:MON-1029; -.
DR BRENDA; 2.8.3.12; 85.
DR SABIO-RK; Q59112; -.
DR UniPathway; UPA00533; UER00686.
DR EvolutionaryTrace; Q59112; -.
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..266
FT /note="Glutaconate CoA-transferase subunit B"
FT /id="PRO_0000157930"
FT ACT_SITE 54
FT HELIX 9..18
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 50..53
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 57..60
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 77..81
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 102..106
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 120..123
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 125..131
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 138..144
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 155..157
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 176..179
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:1POI"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1POI"
FT STRAND 207..212
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 218..223
FT /evidence="ECO:0007829|PDB:1POI"
FT HELIX 242..250
FT /evidence="ECO:0007829|PDB:1POI"
SQ SEQUENCE 266 AA; 29166 MW; 1E691B864237A784 CRC64;
MADYTNYTNK EMQAVTIAKQ IKNGQVVTVG TGLPLIGASV AKRVYAPDCH IIVESGLMDC
SPVEVPRSVG DLRFMAHCGC IWPNVRFVGF EINEYLHKAN RLIAFIGGAQ IDPYGNVNST
SIGDYHHPKT RFTGSGGANG IATYSNTIIM MQHEKRRFMN KIDYVTSPGW IDGPGGRERL
GLPGDVGPQL VVTDKGILKF DEKTKRMYLA AYYPTSSPED VLENTGFDLD VSKAVELEAP
DPAVIKLIRE EIDPGQAFIQ VPTEAK
