ID A0A1W9HSU5_9PROT Unreviewed; 494 AA.
AC A0A1W9HSU5;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 03-MAY-2023, entry version 22.
DE SubName: Full=Pyruvate carboxylase subunit A {ECO:0000313|EMBL:OQW50486.1};
GN ORFNames=A4S09_01450 {ECO:0000313|EMBL:OQW50486.1};
OS Proteobacteria bacterium SG_bin7.
OC Bacteria; Pseudomonadota.
OX NCBI_TaxID=1827384 {ECO:0000313|EMBL:OQW50486.1, ECO:0000313|Proteomes:UP000192385};
RN [1] {ECO:0000313|EMBL:OQW50486.1, ECO:0000313|Proteomes:UP000192385}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG_bin7 {ECO:0000313|EMBL:OQW50486.1};
RX PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT "Comammox in drinking water systems.";
RL Water Res. 116:332-341(2017).
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:OQW50486.1}.
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DR EMBL; LWDK01000030; OQW50486.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W9HSU5; -.
DR STRING; 1827384.A4S09_01450; -.
DR Proteomes; UP000192385; 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 Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
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 PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Pyruvate {ECO:0000313|EMBL:OQW50486.1}.
FT DOMAIN 4..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..319
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 494 AA; 55049 MW; FDEBE2884D07DF96 CRC64;
MNRPIKRLAI ANRGEVAVRI IRACQELDIE TVLLHSEPDV NTLAYRLSDH QICIGPAPAN
ESYLRIQDNI RGALAMGAKA IHPGFGFLSE NAEFARACQK ENLVFIGPTP ENIQTCGDKI
KVKYLAKELG IKTIPGYNGE DQTIDLLVAE CKAIGFPVLV KAAAGGGGRG HKVIHDAASA
KEMIEASQRE AKAAFGSSKV FLEKYLGRAK HIEVQVFGDA IGKIYSLCER ECSVQRKHQK
IIEEGPSAKL NPEEKKKVHE MARKLAERAN YKNAGTVEFL YQDGEFYLIE MNTRLQVEHP
VTEMILSIDL VKSQILTAQG TPLSWNQENL VPRGHSIECR IYAEDPNMGG LPNTGVLKYL
EFPEGPGRRF DLGFEAGDEV TPFYDSMINK IIVWDESRPA AIRKMLRVLD DTIVFGLKTN
IPFLKAILNH HEFISGEMTT QFIEKNFPNA LGPMKLTPEQ TAFAEQAYSQ AGAHNPNPET
SRLQSPWEVL WRNV
//
