ID   E1VHP3_9GAMM            Unreviewed;       992 AA.
AC   E1VHP3;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=Biotin/lipoyl attachment:Carbamoyl-phosphate synthase L chain, ATP-binding {ECO:0000313|EMBL:CBL44335.1};
GN   ORFNames=HDN1F_07520 {ECO:0000313|EMBL:CBL44335.1};
OS   gamma proteobacterium HdN1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria.
OX   NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL44335.1, ECO:0000313|Proteomes:UP000002677};
RN   [1] {ECO:0000313|EMBL:CBL44335.1, ECO:0000313|Proteomes:UP000002677}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA   Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA   Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT   "Alkane degradation by a new type of denitrifying bacterium with possible
RT   involvement of the electron acceptor in substrate activation.";
RL   Environ. Microbiol. 0:0-0(2010).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; FP929140; CBL44335.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1VHP3; -.
DR   STRING; 83406.HDN1F_07520; -.
DR   KEGG; gpb:HDN1F_07520; -.
DR   eggNOG; COG0439; Bacteria.
DR   eggNOG; COG0511; Bacteria.
DR   HOGENOM; CLU_306483_0_0_6; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000002677; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   CDD; cd06850; biotinyl_domain; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 3.40.50.20; -; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 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; PTHR48095:SF4; BIOTIN CARBOXYL CARRIER PROTEIN OF ACETYL-COA CARBOXYLASE; 1.
DR   PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR   Pfam; PF00289; Biotin_carb_N; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02786; CPSase_L_D2; 2.
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; PS50979; BC; 1.
DR   PROSITE; PS00188; BIOTIN; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000313|EMBL:CBL44335.1};
KW   Biotin {ECO:0000256|ARBA:ARBA00023267};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002677}.
FT   DOMAIN          65..648
FT                   /note="Biotin carboxylation"
FT                   /evidence="ECO:0000259|PROSITE:PS50979"
SQ   SEQUENCE   992 AA;  111137 MW;  251CF0C2A4CA10EB CRC64;
     MINANLQQSQ EMRWQDKNET AVASRPRTRF VKQAPRNFYA NNPLIHKNRR RQVGESEWVK
     QFNCEDLRPL IICRGPIRKE VMDVWEEMGI HEYGILLSEK DSITYNSALA PELRQLTRPE
     HVHRVPDYTG VDKEERTQRI NQIIAIAKEN RYDSVFAGYG FMAEDEALVS ALENAGLTFI
     GPCSRTVRDA GAKDEAKRTA LQVNVTVTPG IDNLTALTLL RKASDLAALK TLANAHKLGL
     AESLFDGKLT LEHVADEVLN ASYKRSMDLI SIAEIAKELE IRLQEIFHKY PNNRMRLKAI
     GGGGGKGQRI LAAPSSYNGS LEEQIKQAST KGPELFREIL SEVKTTGVGD NKNVLIELNI
     EVTRHQEIQV IGNGEWCMTL GARDCSVQMH EQKLLEISQT REMLADAIAS AKASGKAAEE
     KALQSDLEIL IRMEEESERF GVAVGLDSVS TFECIVDRDT HFFMEMNTRI QVEHRVSELC
     YTLRFANPKN PEDYFDVDSL VEAMTLLAKF GKQLPKPTRI PRERASVEVR LNATNRALKP
     HAGGIINYWS DAIEGEIRDD QGISLKNPDT GQFIKYHLAG AYDSNVALIL SVGNNRRASY
     ERMAEVLRRT RFVGENLCTN LDFHYGLVHW LLAEHVHAKA TTGFAMPYLT QIGLLKQATN
     RLDIEYAYAQ IKAAYRKRAN QAFAGSDELP AALKAIDSVL DRKNTLLLRP IEMLLEEPHQ
     LSGWLSVNKS SVRFDGDTVV WTKNPIAVLD DTYHYLNMDY REDLPAAACI WKHDSDVLQS
     AVAFYADLQK HLGGGSWETQ QARLADNTVP EGLTEALWSG AQAAHAGYQA GLELLTVLVR
     IAHEVGFYEI KVNADLTITI PERLRDKKLQ DEMLKVLVPP PATKADELVA VCGGMFYGRE
     APGLPAFIQE GDHIEAGQAI YIVEVMKMFN KIYAPFACTI DKLLMENIDG TIVKQGQPLF
     KVTPDERVVE EDPAEVLRRT RTATDRALAG LL
//