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Database: UniProt
Entry: D2RP35_ACIFV
LinkDB: D2RP35_ACIFV
Original site: D2RP35_ACIFV 
ID   D2RP35_ACIFV            Unreviewed;       520 AA.
AC   D2RP35;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=Citrate lyase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE            Short=Citrase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE            EC=2.8.3.10 {ECO:0000256|PIRNR:PIRNR009451};
DE            EC=4.1.3.6 {ECO:0000256|PIRNR:PIRNR009451};
DE   AltName: Full=Citrate (pro-3S)-lyase alpha chain {ECO:0000256|PIRNR:PIRNR009451};
DE   AltName: Full=Citrate CoA-transferase subunit {ECO:0000256|PIRNR:PIRNR009451};
GN   OrderedLocusNames=Acfer_0408 {ECO:0000313|EMBL:ADB46811.1};
OS   Acidaminococcus fermentans (strain ATCC 25085 / DSM 20731 / CCUG 9996 / CIP
OS   106432 / VR4).
OC   Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC   Acidaminococcus.
OX   NCBI_TaxID=591001 {ECO:0000313|EMBL:ADB46811.1, ECO:0000313|Proteomes:UP000001902};
RN   [1] {ECO:0000313|EMBL:ADB46811.1, ECO:0000313|Proteomes:UP000001902}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25085 / DSM 20731 / CCUG 9996 / CIP 106432 / VR4
RC   {ECO:0000313|Proteomes:UP000001902};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + citrate = (3S)-citryl-CoA + acetate;
CC         Xref=Rhea:RHEA:19405, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57288, ChEBI:CHEBI:57321; EC=2.8.3.10;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009451};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=citrate = acetate + oxaloacetate; Xref=Rhea:RHEA:10760,
CC         ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:30089; EC=4.1.3.6;
CC         Evidence={ECO:0000256|PIRNR:PIRNR009451};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRNR:PIRNR009451}.
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DR   EMBL; CP001859; ADB46811.1; -; Genomic_DNA.
DR   RefSeq; WP_012937801.1; NZ_CP085936.1.
DR   AlphaFoldDB; D2RP35; -.
DR   STRING; 591001.Acfer_0408; -.
DR   GeneID; 78334163; -.
DR   KEGG; afn:Acfer_0408; -.
DR   eggNOG; COG3051; Bacteria.
DR   HOGENOM; CLU_046521_2_0_9; -.
DR   OrthoDB; 9767643at2; -.
DR   Proteomes; UP000001902; Chromosome.
DR   GO; GO:0009346; C:ATP-independent citrate lyase complex; IEA:UniProtKB-UniRule.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008815; F:citrate (pro-3S)-lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008814; F:citrate CoA-transferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.1080.10; Glutaconate Coenzyme A-transferase; 2.
DR   InterPro; IPR006472; Citrate_lyase_asu.
DR   InterPro; IPR037171; NagB/RpiA_transferase-like.
DR   NCBIfam; TIGR01584; citF; 1.
DR   PANTHER; PTHR40596; CITRATE LYASE ALPHA CHAIN; 1.
DR   PANTHER; PTHR40596:SF1; CITRATE LYASE ALPHA CHAIN; 1.
DR   Pfam; PF04223; CitF; 1.
DR   PIRSF; PIRSF009451; Citrt_lyas_alpha; 1.
DR   SUPFAM; SSF100950; NagB/RpiA/CoA transferase-like; 2.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|PIRNR:PIRNR009451};
KW   Lyase {ECO:0000256|PIRNR:PIRNR009451, ECO:0000313|EMBL:ADB46811.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001902};
KW   Transferase {ECO:0000256|PIRNR:PIRNR009451}.
SQ   SEQUENCE   520 AA;  55661 MW;  51B1C7036B28727D CRC64;
     MKNAVGREIP EEILKLTGKE AFAGSYAKHQ AVYQAATHKV APVIDPNYSK VVDSIEEVLK
     KCGIKDGMTL GFHHHFREGD YVVNMVMEAV HKMGIKDLTI CATSLGKAQN AIVPMIEDGT
     ITNIQASGVR GKIGEAISNG KLKGLAIMRS HGGRVRAIES GETHIDISFI GAPSADDMGN
     CRAIGSQNGA DCGVLGYAAI DAQYADKVVV VTDTLVPFPN VPASIDMTNV DYVVKVDAIG
     DPTKIATGAA KPTTDQRKLL MAKYAADFMV HTPWYKDGFI YQTGVGGASI ASTKFLAEHL
     RKDNIHIGVA MGGIAQAICE LQHEGLIDKI ADTQDFDMAS IEDIKTNPNH YEITTSQYAD
     PFNKGAYVNK LDYVILGALE VDTHFNVNVV VGSDGVITGA QGGHPDTAAG AKCTIVIAPL
     LQGRIPAICT ECTTVTTPGE TVDVVVTDYG IAINPRRQDI IDAVKDTDLP ICTIEELRDT
     AYKMVGTPDP VQFGDRIVGI IEARDGSVMD VVRQVKKAEF
//
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