ID A0A0A0DQK4_9BURK Unreviewed; 670 AA.
AC A0A0A0DQK4;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Carbamoyl-phosphate synthase subunit L {ECO:0000313|EMBL:KGM40260.1};
GN ORFNames=JY96_10065 {ECO:0000313|EMBL:KGM40260.1};
OS Aquabacterium sp. NJ1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Aquabacterium.
OX NCBI_TaxID=1538295 {ECO:0000313|EMBL:KGM40260.1, ECO:0000313|Proteomes:UP000029993};
RN [1] {ECO:0000313|EMBL:KGM40260.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM40260.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Masuda H.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KGM40260.1, ECO:0000313|Proteomes:UP000029993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJ1 {ECO:0000313|EMBL:KGM40260.1,
RC ECO:0000313|Proteomes:UP000029993};
RA Shiwa Y., Yoshikawa H., Zylstra G.J.;
RT "The draft genome sequence of a soil bacterium, Aquabacterium sp. strain
RT NJ1, capable of utilizing both liquid and solid n-alkanes.";
RL Submitted (OCT-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:KGM40260.1}.
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DR EMBL; JRKM01000001; KGM40260.1; -; Genomic_DNA.
DR RefSeq; WP_035037085.1; NZ_JRKM01000001.1.
DR AlphaFoldDB; A0A0A0DQK4; -.
DR STRING; 1538295.JY96_10065; -.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000029993; 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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000029993}.
FT DOMAIN 1..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 589..664
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 670 AA; 72453 MW; 38543DAE78A65592 CRC64;
MLKKILIANR GEIACRVIRT ARKLGYRTVA VFSEADAQAP HVSLADEAVC IGPAPAAESY
LKVDALLEAC RKTGANAIHP GYGFLSENAG FAQACADAGV IFIGPSPEAI RVMGDKAGAK
KEMIRAGVPT APGYLGADQN DETLIAEGKR LGFPLLVKAV SGGGGRGMRL VHQADELQQA
ITSARREAQS AFGDGTLMLE RLVLDGRHIE IQVFADSHGN AVYIGERDCT AQRRRQKVIE
ESPSPVVSPA MREAMGRDAV LAAKAINYCG AGTIEYIVDQ DLNYYFLEMN TRLQVEHPVT
EMISGLDLVE WQLRVAAGQP LPLKQEEIKL QGHAIEARLY TEDPYAGFAP QTGDIAWWRP
TQALYDGVRI DDGIVEGGTV TPHYDPMVAK LIVHGRDRDD AIRRLITTLD DAPLLGLKHN
ARFLRDLIDH PRFRAGTMTT TLIDQWQTDN EAILQRPVAT DEAWLVAAAV IAARTQHKAV
GTHAPALRAD SVSGFDVPLA CDGAKRTLRV QGQRNGRFLV SLTPTDTPHD LRLINHDTSA
RGGVLRYELD GVQRSLLAVW CEGSAGDELH VVQQASTFVF NEVSAWPDAG NAADPSRALS
PVAGTVAQVL VKAGDTVVAD QPLLSIEAMK MEMWLSAQAP GVIKAVYVQA GEQVQAKTLL
IDIELTTKES
//
