ID A0A095AXB5_9SPHN Unreviewed; 613 AA.
AC A0A095AXB5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
DE SubName: Full=Carbamoyl-phosphate synthase L chain, ATP-binding protein {ECO:0000313|EMBL:KGB54124.1};
GN ORFNames=FG91_02373 {ECO:0000313|EMBL:KGB54124.1};
OS Sphingopyxis sp. LC81.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=1502850 {ECO:0000313|EMBL:KGB54124.1, ECO:0000313|Proteomes:UP000029574};
RN [1] {ECO:0000313|EMBL:KGB54124.1, ECO:0000313|Proteomes:UP000029574}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LC81 {ECO:0000313|EMBL:KGB54124.1,
RC ECO:0000313|Proteomes:UP000029574};
RA Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT isolate.";
RL Submitted (MAY-2014) 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:KGB54124.1}.
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DR EMBL; JNFD01000021; KGB54124.1; -; Genomic_DNA.
DR RefSeq; WP_037515141.1; NZ_JNFD01000021.1.
DR AlphaFoldDB; A0A095AXB5; -.
DR STRING; 1502850.FG91_02373; -.
DR PATRIC; fig|1502850.3.peg.2397; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000029574; 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; 3.30.470.20; 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; 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 1..450
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..322
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 533..609
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 613 AA; 65186 MW; 33AB0C3E08E17BF6 CRC64;
MIQSLLIANR GEIACRIIRT ARDMGIRTVA VYSDADARAL HVREADEAVH IGPSPARESY
LIGEKIIAAA KATGAEAIHP GYGFLSENAE FAQAVADAGL VWVGPKPSSI TAMGLKDAAK
KLMADAGVPV TPGYMGENQD PAFLAEQAAG IGYPVLIKAV AGGGGKGMRK VDAAADFLDA
LASCQREAAA SFGNDHVLIE KYILTPRHIE VQVFGDTHGN VVHLFERDCS LQRRHQKVIE
EAPAPGMDEA TRADLCAAAV RAAKAVDYVG AGTIEFIADA SEGLRADRIW FMEMNTRLQV
EHPVTEEITG VDLVEWQLRV ASGEPIPLAQ DELAINGWAM EARLYAEDPA KGFLPSIGTL
ELFQLPEHIG RVDTGVYEGA EVSPFYDPMI AKVIAWGEDR EEARELLSEM LEDSAIWPVK
TNSAFLINAL DHPDFVAGTV DTGLIGRDGD AMTEEPVPTA QALTNAAMAM VPRSLQSGFR
LNAPDVRSAP FLLDGKRVEV ELHGPGAEEP SPAMLVAESG SVWQLTPWRA EASAGSGAGD
GAILSPMPGK VIAVEVAAGD KVTKGQKLLT LEAMKMEHSL TAPFDGVVAE LNAAAGAQVQ
VEALLVRIEK EDA
//
