ID A0A1M6PCI0_9CLOT Unreviewed; 512 AA.
AC A0A1M6PCI0;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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 ORFNames=SAMN02745912_02102 {ECO:0000313|EMBL:SHK05663.1};
OS Paramaledivibacter caminithermalis DSM 15212.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Paramaledivibacter.
OX NCBI_TaxID=1121301 {ECO:0000313|EMBL:SHK05663.1, ECO:0000313|Proteomes:UP000184465};
RN [1] {ECO:0000313|EMBL:SHK05663.1, ECO:0000313|Proteomes:UP000184465}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15212 {ECO:0000313|EMBL:SHK05663.1,
RC ECO:0000313|Proteomes:UP000184465};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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; FRAG01000023; SHK05663.1; -; Genomic_DNA.
DR RefSeq; WP_073149620.1; NZ_FRAG01000023.1.
DR AlphaFoldDB; A0A1M6PCI0; -.
DR STRING; 1121301.SAMN02745912_02102; -.
DR OrthoDB; 9767643at2; -.
DR Proteomes; UP000184465; Unassembled WGS sequence.
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:SHK05663.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184465};
KW Transferase {ECO:0000256|PIRNR:PIRNR009451, ECO:0000313|EMBL:SHK05663.1}.
SQ SEQUENCE 512 AA; 55489 MW; B6ABF9475F9C7E41 CRC64;
MKNSIGREIP EKIVGYDKFK CYCSPFIKEP VGRKASPKLR QVKPGDKKVV NSLEEAIKKA
GLKDGMTISF HHHFRNGDYI INMVMDKIAE MGIKDITIAP SSLTTVHETL VEHVKSGVIS
GIYTSGVRGK LAEEISKGIM EKPIIIRSHG GRARAIEAGE IHIDVAFLGV PSCDEYGNAS
GKGAKTICGS LGYAKVDAKY ADTVVLITDD LVCYPNFPAS ISQTDVDYVV VVDSIGDPNG
IASGATRYTK NPKELLIAKY ASKVIVNSGY FKEGFSFQTG SGGSSLAVTR FLKEIMKDRG
IKAKFALGGI TKPMVELYEE GLIEHLFDTQ TFDLVSCESI FQNPNHHEID ASMYANPHNK
GSFVNKLDVV ILSALEIDTS FNVNVITGSD GVIRGASGGH SDTAAGSKMS IIVAPLIRGR
IPTVVDNVNT VVTPGETVDV LVTDRGIAIN PKRKDLMENL KNKGLPIVTI EELRDMALKI
AGKPKPIEYT DKVVGVVEYR DGSIIDVIRQ IK
//