ID K4KUF6_SIMAS Unreviewed; 672 AA.
AC K4KUF6;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE SubName: Full=Carbamoyl-phosphate synthase L chain, ATP-binding protein {ECO:0000313|EMBL:AFU97597.1};
GN OrderedLocusNames=M5M_01890 {ECO:0000313|EMBL:AFU97597.1};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU97597.1, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFU97597.1, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP003746; AFU97597.1; -; Genomic_DNA.
DR RefSeq; WP_015045770.1; NZ_ATUQ01000003.1.
DR AlphaFoldDB; K4KUF6; -.
DR STRING; 1117647.M5M_01890; -.
DR KEGG; saga:M5M_01890; -.
DR eggNOG; COG4770; Bacteria.
DR HOGENOM; CLU_000395_3_1_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000000466; 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:UP000000466}.
FT DOMAIN 1..447
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..316
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 582..656
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 672 AA; 72873 MW; EC5DD15773E6863C CRC64;
MKRLLIANRG EIACRIIRTA KSLGIETVAV YSEADQHALH TQLADRRVCI GAAAAAQSYL
NIPAIIAAAS ETQADAIHPG YGFLSENAEF ARAVCNAGLI FVGPPADAIE LMGDKRAAKQ
AVEAVVVPLL PGYNGADQSL DTLLAKAADI GLPLMIKASA GGGGKGMRLA TDQQALKDAI
ASAKREALAA FGNDTLLLER ALIDPRHVEV QVFADQQGHC VYLGDRDCSL QRRHQKVVEE
APAPGLSDDL RQRMGEAAVR AAQACNYVGA GTVEFLLDHD QNFYFLEMNT RLQVEHPVTE
KIFGLDLVQW QLAVAQGTPL PLSQAALRPE GHAIEVRLYA EDPLNDFLPQ TGEILHWPDD
NGQTRDARID HCLFTGLTIG NHYDPMLGKL IAHGATREQA IERLIQLIEQ TPLLGLHHNL
GYLRSVLSQP AFKAADLGTG FLSRHAAILS QSAEKKAALQ LAALNFFLQA QPSKDSGTGN
WYKNLSALAF PSRYKLKLHA DDAHTTITLD SKNWPKGELL LTDADIEYKI DQIHQYQNHK
AILLHCRIDG VSYKAWITQQ GNGLWLQLNG QSFEIHPSNP LATTHTKTGG LNAPMDGRVV
ACLVAPDSTV AEGDTLMIIE AMKMEMPIRA NTSGCVELLC NAGDQIRTGQ ALAVIHTNHT
ETQSPEEATH AS
//
