ID D1P5I0_9GAMM Unreviewed; 580 AA.
AC D1P5I0;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Carbamoyl-phosphate synthase L chain, ATP binding domain protein {ECO:0000313|EMBL:EFB71304.1};
GN ORFNames=PROVRUST_07486 {ECO:0000313|EMBL:EFB71304.1};
OS Providencia rustigianii DSM 4541.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=500637 {ECO:0000313|EMBL:EFB71304.1, ECO:0000313|Proteomes:UP000005512};
RN [1] {ECO:0000313|EMBL:EFB71304.1, ECO:0000313|Proteomes:UP000005512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4541 {ECO:0000313|EMBL:EFB71304.1,
RC ECO:0000313|Proteomes:UP000005512};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (DEC-2009) 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:EFB71304.1}.
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DR EMBL; ABXV02000040; EFB71304.1; -; Genomic_DNA.
DR RefSeq; WP_006815498.1; NZ_GG703819.1.
DR AlphaFoldDB; D1P5I0; -.
DR STRING; 500637.PROVRUST_07486; -.
DR GeneID; 76392194; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_6_6; -.
DR Proteomes; UP000005512; 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; 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; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_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; PF00364; Biotin_lipoyl; 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 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; 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}.
FT DOMAIN 8..453
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 123..324
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 506..580
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 580 AA; 63108 MW; B3F66ED25AD659E4 CRC64;
MKTNKNNPVH KVLIANRGEI AVRIIRACRD YGFASVAVYA DSDIDALHVT MANEAFGLGG
NTPAQSYLNI EKLIEIAKKS GATMVHPGYG FLSERSEFAR AVQQAGLIWI GPSPESIDTL
GDKVQARHIA LQVGAPLVVG TKNPVKEASE VVEFAHQHGL PIAIKAAFGG GGRGLKVAWQ
MHEVEELYHS AVREATAAFG RGECFIEQFL HNPRHIEAQV IADTHGNVVV VGTRDCSLQR
RNQKLVEESP APFLSDALEQ QIIRASTDIC RQAGYVGAGT VEFLLSQEGM LSFLEVNTRL
QVEHPVTEET AGIDLVIEQL RIAEGLPLSI LETPVPRGHA FEFRINAEDA GNGFLPTPGT
IIRFDAPSGP GVRLDSGVVA GTTIPGTFDS LMAKLIVVGS TREQAIVRAR RALAEFNIEG
VASVLPFHRA VIDHHDFCEQ FKVHTRWIET EFNVEIPPAK KQLPQVNQDL TRTFIEIDGK
RCELGLPAQL FSGMAVTQNI AVQEAHIADN SPYNVNAPIS GILFNWLVPQ GDKVLEGDVI
GVMEAMKMEV QVIAHRSGQL QYAANQGDFI SADCKIAEII
//
