ID D0LYT5_HALO1 Unreviewed; 700 AA.
AC D0LYT5;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding protein {ECO:0000313|EMBL:ACY14405.1};
GN OrderedLocusNames=Hoch_1857 {ECO:0000313|EMBL:ACY14405.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY14405.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY14405.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001804; ACY14405.1; -; Genomic_DNA.
DR RefSeq; WP_012827013.1; NC_013440.1.
DR AlphaFoldDB; D0LYT5; -.
DR STRING; 502025.Hoch_1857; -.
DR KEGG; hoh:Hoch_1857; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_3_7; -.
DR OrthoDB; 9769961at2; -.
DR Proteomes; UP000001880; Chromosome.
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}; Reference proteome {ECO:0000313|Proteomes:UP000001880}.
FT DOMAIN 3..448
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 122..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 613..688
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 700 AA; 74086 MW; B3E3B8CC5584DE8B CRC64;
MKPLRTILVA NRGEIAVRIL RTCRRMGLAT VAVFSDADED APHVEAADEA VRLGPAPAAE
SYLDHERVLA AAAATGADAI HPGYGFLSEN AAFARACGER GVVFIGPSAE VIAQLGSKRE
AKRAAAAAGV PVVPGYDGDE QETEALAARV RELGGPILVK ASAGGGGKGM RIVRPGEDAS
AAIDAARREA QSAFGDATLL LERYIERPRH VEIQILGDAH GNVVHLYERE CSIQRRHQKI
IEEAPAVGEE LRARMGAAAV AVARAVGYQN AGTVEFIVAP DGAFYFLEVN TRLQVEHPVT
ECVTGLDLVR EQIRIAAGEP LALGELPLRG AAIECRLYAE DADNQFLPAI GRVVDWHLPE
RLAEFAGVRV DAGVRAGQDI GVHYDPMLAK IISHAPTRAE AAARLARYLR EMSVQGVVTN
RAFLVRVLEH PAFLAGEVHT HFLAEHAEAL RADSEPGAGD ARVREAAIAA ALVAHERRRS
DRSLLPALEP GFRNNRFADE LVCYAAGARR VEVRYGNLGG GRFRVHAAIV AADSQDSADA
SAEAASEPSV VRVLRCADTE LRLEDAEGVR RSFRVVAGAT DGIPGSGERP PRWFVHTLAG
DVALSEEPRF PSERAAAQPG SLSAPMPGRI IAVHVSEGDA VRAGQTLLVL EAMKMEHALV
APGDGTLSSL AAAVGDQVDA GDVLAVVAPH ADDASTSDDA
//
