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Database: UniProt
Entry: A0A1H1V5F1_9FLAO
LinkDB: A0A1H1V5F1_9FLAO
Original site: A0A1H1V5F1_9FLAO 
ID   A0A1H1V5F1_9FLAO        Unreviewed;      1150 AA.
AC   A0A1H1V5F1;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   05-DEC-2018, entry version 13.
DE   RecName: Full=Pyruvate carboxylase {ECO:0000256|PIRNR:PIRNR001594};
DE            EC=6.4.1.1 {ECO:0000256|PIRNR:PIRNR001594};
GN   ORFNames=SAMN04489797_2453 {ECO:0000313|EMBL:SDS79923.1};
OS   Winogradskyella sp. RHA_55.
OC   Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=1249933 {ECO:0000313|EMBL:SDS79923.1, ECO:0000313|Proteomes:UP000198963};
RN   [1] {ECO:0000313|EMBL:SDS79923.1, ECO:0000313|Proteomes:UP000198963}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RHA_55 {ECO:0000313|EMBL:SDS79923.1,
RC   ECO:0000313|Proteomes:UP000198963};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes a 2-step reaction, involving the ATP-dependent
CC       carboxylation of the covalently attached biotin in the first step
CC       and the transfer of the carboxyl group to pyruvate in the second.
CC       {ECO:0000256|PIRNR:PIRNR001594}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + pyruvate = ADP + H(+) +
CC         oxaloacetate + phosphate; Xref=Rhea:RHEA:20844,
CC         ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:456216; EC=6.4.1.1;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|PIRNR:PIRNR001594};
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DR   EMBL; LT629774; SDS79923.1; -; Genomic_DNA.
DR   Proteomes; UP000198963; Chromosome i.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009374; F:biotin binding; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:InterPro.
DR   GO; GO:0006090; P:pyruvate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR005481; BC-like_N.
DR   InterPro; IPR001882; Biotin_BS.
DR   InterPro; IPR011764; Biotin_carboxylation_dom.
DR   InterPro; IPR005482; Biotin_COase_C.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR003379; Carboxylase_cons_dom.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   InterPro; IPR000891; PYR_CT.
DR   InterPro; IPR005930; Pyruv_COase.
DR   InterPro; IPR011054; Rudment_hybrid_motif.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   Pfam; PF02785; Biotin_carb_C; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 1.
DR   Pfam; PF00682; HMGL-like; 1.
DR   Pfam; PF02436; PYC_OADA; 1.
DR   PIRSF; PIRSF001594; Pyruv_carbox; 1.
DR   SMART; SM00878; Biotin_carb_C; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 1.
DR   TIGRFAMs; TIGR01235; pyruv_carbox; 1.
DR   PROSITE; PS50975; ATP_GRASP; 1.
DR   PROSITE; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
DR   PROSITE; PS50991; PYR_CT; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Biotin {ECO:0000256|PIRNR:PIRNR001594};
KW   Complete proteome {ECO:0000313|Proteomes:UP000198963};
KW   Ligase {ECO:0000256|PIRNR:PIRNR001594};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001594-3};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR001594,
KW   ECO:0000256|PIRSR:PIRSR001594-2, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:SDS79923.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198963}.
FT   DOMAIN        2    455       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      122    319       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      533    802       Pyruvate carboxyltransferase.
FT                                {ECO:0000259|PROSITE:PS50991}.
FT   DOMAIN     1071   1150       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   ACT_SITE    294    294       {ECO:0000256|PIRSR:PIRSR001594-1}.
FT   METAL       542    542       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       712    712       Divalent metal cation; via carbamate
FT                                group. {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       741    741       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   METAL       743    743       Divalent metal cation.
FT                                {ECO:0000256|PIRSR:PIRSR001594-3}.
FT   BINDING     118    118       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     202    202       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     237    237       ATP. {ECO:0000256|PIRSR:PIRSR001594-2}.
FT   BINDING     614    614       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
FT   BINDING     876    876       Substrate. {ECO:0000256|PIRSR:
FT                                PIRSR001594-2}.
SQ   SEQUENCE   1150 AA;  129821 MW;  369EE28808271632 CRC64;
     MKIKKILVAN RSEIAIRVLR ACTELNIATV AIYTYEDRYS QHRNKADESY QIGEDNDPLK
     PYLNIEEIVA LAKSKHVDAI HPGYGFLSEN SEFARRCAEN DIIFIGPDPE VMDALGDKIT
     AKKIALKCNV PIIESNKKDL TALKIALSEA NTIGYPLMLK AASGGGGRGM RVVRNDKDLE
     QHFDSAKNEA LNAFGDDTMF LEKYVENPKH IEVQIVADRH GNIRHLFERD CSVQRRHQKV
     VEVAPSYNVS QKVKDALYKY AVDITTEVNF NNIGTVEFLV DPQDNIYFIE VNPRIQVEHT
     VTEMVTGVDL VKTQIFVAGG YKLSDKQIKI YEQDALATYG YALQCRLTTE DPENNFTPDY
     GNITTYRSAS GMGIRLDAGS IYQGYNVSPF FDSMLVKVSA QGRTLDGAVR KMVRALKEFR
     IRGVKTNIHF LQNVIQHNTF KEGKVTVNFI QNTPSLFEIK LPQDRTTKAV NFLAEVIVNG
     NSDVKHIDKT KVFRTAKVPK YNRNEAFPDG TKNRLTELGP EAFCQWLKDD YKIHYTDTTM
     RDAHQSLLAT RMRSYDMLKV AESFAKNHPN TFSMEVWGGA TFDVCYRFLH ESPWTRLREL
     RKAVPNILFQ MLLRGSNAVG YKAYPDNLIE KFVEKSWENG VDIFRIFDSL NWVKAMEPSI
     NYVRTKTGGI AQAAISYTGD ILDPKQTKYN LKYYTQLAKD LENAGAHMIA IKDMAGLLKP
     YAATELVGAL KDTLQIPVHL HTHDTSSLQT ATYLKAIEAG VDVVDVALGG LSGLTSQPNF
     NAVVEMMKGQ DRAHDFDMTN LNQFSNYWED TREMYYPFES GLKAGTAEVY QHEIPGGQYS
     NLRPQAIALG LGDRFDEVKK MYAQVNTMFG NLVKVTPSSK VVGDMAIFMV TNNLTPEDVM
     QRGETISFPE SVINFFKGDL GQPVGGFPKD LQKIILKNRE AYTDRPNAHL KPVDFTKEFA
     AFKKKFQQGF TRPIEIEDFL SFMLYPKVFE TAHENYKKYG NIALIPTKDF FFGMQLQEET
     KITLEPGKTI IVKLLSVSIP NDNGIRTVFF RVNGENRFVE IFDTSLNIKK VENIKIDPDN
     NNHVGAPLQG SLYKVLVKKG ETVKENDPLF VIEAMKMETT VTAHKSGKIK SVSLSEGSMV
     GQDDLVITME
//
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