ID A8M8K3_SALAI Unreviewed; 674 AA.
AC A8M8K3;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding {ECO:0000313|EMBL:ABW00522.1};
GN OrderedLocusNames=Sare_4768 {ECO:0000313|EMBL:ABW00522.1};
OS Salinispora arenicola (strain CNS-205).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Salinispora.
OX NCBI_TaxID=391037 {ECO:0000313|EMBL:ABW00522.1};
RN [1] {ECO:0000313|EMBL:ABW00522.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CNS-205 {ECO:0000313|EMBL:ABW00522.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Jensen P.R., Moore B.S., Penn K., Jenkins C.,
RA Udwary D., Xiang L., Gontang E., Richardson P.;
RT "Complete sequence of Salinispora arenicola CNS-205.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000850; ABW00522.1; -; Genomic_DNA.
DR AlphaFoldDB; A8M8K3; -.
DR STRING; 391037.Sare_4768; -.
DR KEGG; saq:Sare_4768; -.
DR PATRIC; fig|391037.6.peg.4819; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_3_11; -.
DR OrthoDB; 249215at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004075; F:biotin carboxylase activity; IEA:UniProtKB-EC.
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; 3.30.470.20; ATP-grasp fold, B domain; 1.
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; 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:SF126; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 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; 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}; 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 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 115..306
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 592..667
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 674 AA; 70460 MW; 45B4DABC8F4B98F9 CRC64;
MISRLLVANR GEIARRIFTT CRALGIGTVA VHSDADADAA FVAEADHAVR LPGNTPGETY
LRIDLVLDAA RRAGADAVHP GYGFLAENAE FATAVTDAGL TWVGPPAKAI AAMGDKLAAK
TLLAEAGVPM LPSWTEPDQV SGFPVLVKAS AGGGGRGMRV VRAADGLADA VASARREAAS
AFGDGTVFIE RYVERGRHVE VQILGDRFGT VTALGARDCS IQRRHQKIVE EAPGVLAPEV
RQRLHEAATA AGRAVDYVGA GTVEFLLAPD GDIFFLEMNT RLQVEHPVTE LTTGLDLVRL
QLLVAEGAPL PITTPPPTTG HAIEVRLCAE DPTQGYRPAT GTLHRFTVPA VATEFGPLTG
PGLRLDSGVT DGSVVSVHYD SMLAKVISWA PTRDEAARAL AGALARAELH GVATNRDLLV
RILRSPEFAA VDIDTGFLDR HPEVFAPLLP PEELPVAAVA AALASAADRR ASAPVLAGLP
SGWRNVSAFP QVTRYAGPDG GEIEVRYRLD RRGALAEWSV APGDDPPAAG DAAFPAGVAP
ALTLVEAHPD RVVLDVTGVR RTYRVHRVGP EVFVDSPDGA LGLTELPRFP LPGAELAAGS
LLAPLPGTVT RVHVELSQRV AAGDLLLTLE AMKLEHPVLA PTDGVVAELP VPAGGQVETG
AVLAVVNPDE EAQS
//
