ID A0A095UGW7_9GAMM Unreviewed; 1089 AA.
AC A0A095UGW7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Pyruvate carboxylase {ECO:0000313|EMBL:KGD61730.1};
GN ORFNames=T9A_00939 {ECO:0000313|EMBL:KGD61730.1};
OS Alcanivorax jadensis T9.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177181 {ECO:0000313|EMBL:KGD61730.1, ECO:0000313|Proteomes:UP000029443};
RN [1] {ECO:0000313|EMBL:KGD61730.1, ECO:0000313|Proteomes:UP000029443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T9 {ECO:0000313|EMBL:KGD61730.1,
RC ECO:0000313|Proteomes:UP000029443};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax jadensis T9.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:KGD61730.1}.
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DR EMBL; ARXU01000003; KGD61730.1; -; Genomic_DNA.
DR RefSeq; WP_035245613.1; NZ_ARXU01000003.1.
DR AlphaFoldDB; A0A095UGW7; -.
DR STRING; 1177181.T9A_00939; -.
DR PATRIC; fig|1177181.3.peg.938; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG4799; Bacteria.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000029443; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR034733; AcCoA_carboxyl_beta.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
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; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR011763; COA_CT_C.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR48095:SF5; BLL7292 PROTEIN; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF01039; Carboxyl_trans; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 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; PS50989; COA_CT_CTER; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:KGD61730.1}.
FT DOMAIN 4..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..320
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 476..554
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 836..1073
FT /note="CoA carboxyltransferase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50989"
SQ SEQUENCE 1089 AA; 114888 MW; 840AAC7309D9CBB2 CRC64;
MPVPFSAVLI ANRGEIAIRI ANACADLGIR SVGVFAQDDQ ASLHTRQVDE AVALAGRGVP
AYLDGAQLIA IANAQGCEAI HPGYGFLAEN ADFADQCAEA GITLIGPGAE TLRLFGDKAA
ARALAAKCQV PLVQGSAQAV SLEEAKAFMA SLDGSGVMVK ALSGGGGRGM RAVTDPAELE
AAYARCQSEA KAAFGNDAVY VEQLVESARH IEVQVLGDGS GSVSHLWERD CTLQRRHQKL
VEFAPAPGLD TALRDRIIHS ALTLAAEVNY RGIGTFEFLV EAEQGRFYFM EANPRVQVEH
TVTEQVTGMD LVQSQIWLAA GASLVDLNLE TAPACEGMAV QLRLNLETLK ADGSTTPAAG
TLTTYEPASG PGIRVDGYGY AGYPVSPAYD SLLAKLIVTG ADYAAVLQRA RRALKQTRID
GVQSNLRLLQ ALLASDAVQA NTVTTRYVES HLAALLDAMP AEPTAALPSA DHSPQADTLT
TPAGCEALAS PTTGVLLSLL VQEGSTVQVG QVVAVLEAMK MEFEVRATTA GEVHSLAAVE
GDAINEAAPL LFVQPGDVDG SEIATEESVD LEHIRKDLAE VLDRHQAISD AGRPQAVEKR
HRKGKRTARE NLDDLLDSGS FQEYGAMALA AQRRRRSAEE LQAMSPADGL IGGTGTVNAD
QVGEQAARVM AMSYDYTVFA GTQGMMNHKK TDRLLQLAGQ WKMPLVLFAE GGGGRPGDTD
FVGVAGLDCH TFAAMAALSG QVPLVGIGSG RCFAGNAALL GCCDVIIATR DASIGMAGPA
MIEGGGLGRF TPEQVGPVSV QGPNGVADVI VEDEAEAVAV AKQYLSYFQG PVSDWQAVDQ
RELRHRIPEK RTRVYDIRHV IDTLADSGSV LELRREFAPG MITALVRIEG RPFGLIANNP
GDLGGAIDAV GGDKAARFMQ LCEAFGLPMV SLCDTPGFMV GPEAEKQATV RHVSRMFVTA
ASLTVPFFTL VLRKGYGLGA QAMAAGSFHS PLFTAAWPSA EFGAMGLEGA VRLGFAKELA
AQPSPEKQQR LFDKLVAKAY QQGKALNMAS FLEIDAVIDP VESRQWLLRG LNASGHRGGS
GGRPFVDTF
//
