ID K6ZMM0_9ALTE Unreviewed; 591 AA.
AC K6ZMM0;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Pyruvate carboxylase subunit B {ECO:0000313|EMBL:GAC30133.1};
GN Name=pycB {ECO:0000313|EMBL:GAC30133.1};
GN ORFNames=GPAL_3285 {ECO:0000313|EMBL:GAC30133.1};
OS Glaciecola pallidula DSM 14239 = ACAM 615.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Glaciecola.
OX NCBI_TaxID=1121922 {ECO:0000313|EMBL:GAC30133.1, ECO:0000313|Proteomes:UP000006251};
RN [1] {ECO:0000313|EMBL:GAC30133.1, ECO:0000313|Proteomes:UP000006251}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACAM 615 {ECO:0000313|EMBL:GAC30133.1,
RC ECO:0000313|Proteomes:UP000006251};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAC30133.1}.
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DR EMBL; BAEQ01000053; GAC30133.1; -; Genomic_DNA.
DR RefSeq; WP_006013917.1; NZ_KE386815.1.
DR AlphaFoldDB; K6ZMM0; -.
DR STRING; 1121922.GCA_000428905_01009; -.
DR OrthoDB; 9760256at2; -.
DR Proteomes; UP000006251; Unassembled WGS sequence.
DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro.
DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProt.
DR GO; GO:0071704; P:organic substance metabolic process; IEA:UniProt.
DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR CDD; cd07937; DRE_TIM_PC_TC_5S; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001882; Biotin_BS.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003379; Carboxylase_cons_dom.
DR InterPro; IPR005776; OadA.
DR InterPro; IPR000891; PYR_CT.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR01108; oadA; 1.
DR PANTHER; PTHR45266; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR PANTHER; PTHR45266:SF3; OXALOACETATE DECARBOXYLASE ALPHA CHAIN; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF00682; HMGL-like; 1.
DR Pfam; PF02436; PYC_OADA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF89000; post-HMGL domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS50991; PYR_CT; 1.
PE 4: Predicted;
KW Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Pyruvate {ECO:0000313|EMBL:GAC30133.1}.
FT DOMAIN 5..265
FT /note="Pyruvate carboxyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS50991"
FT DOMAIN 512..591
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 591 AA; 64012 MW; B371DB95D6761FA3 CRC64;
MSNPLKITEL VLRDAHQSLL ATRMRLDDML PIAAKLDDVG YWSVESWGGA TFDACIRYLG
EDPWERIRAL KAAMPKTKQQ MLLRGQNLLG YRHYADDVVE KFVERAHANG VDVFRIFDAM
NDVRNLETAV KSAIKVGAHA QGTISYTVSP VHNLTLWLDM AKRLEDMGVH SICIKDMAGL
LKPYDCEALI TGLKKSVNVP IAMQCHATTG LSTATYQKAV DAGIDMLDTA VSSMSMTYGH
TATETMVSIV EGTNRDTGLD IEKLAEIAAY FRVVRKKYAQ FEGSLKGVDA RILIAQVPGG
MLTNMESQLR EQGAEDKFDE VLLEIPRVRE DLGFIPLVTP TSQIVGTQAV LNVLTGERYK
SITKETAGVL KGEYGATAAP VNKELQTRVL EGGKAITCRP ADEIAPELVK LEEELDALIE
QKSLRIAKDK IDDVLTYALF PQVGLKFIEN RDNPSAFEPA PTQESAVIEA TSAEPLAGDA
GAYKVRVEGQ VYHVEVAENG EVSNIAAASN SPASAPAPVG EGTDVAAPLS GNILKILVAQ
GQQINEGDVI LILEAMKMET EVRSAVSGVV QQIIAKEGDA VQAGQTMMVI G
//
