(data stored in ACNUC7421 zone)

SWISSPROT: B4SSL9_STRM5

ID   B4SSL9_STRM5            Unreviewed;       660 AA.
AC   B4SSL9;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   08-MAY-2019, entry version 64.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain ATP-binding {ECO:0000313|EMBL:ACF49901.1};
GN   OrderedLocusNames=Smal_0196 {ECO:0000313|EMBL:ACF49901.1};
OS   Stenotrophomonas maltophilia (strain R551-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Stenotrophomonas;
OC   Stenotrophomonas maltophilia group.
OX   NCBI_TaxID=391008 {ECO:0000313|EMBL:ACF49901.1, ECO:0000313|Proteomes:UP000001867};
RN   [1] {ECO:0000313|EMBL:ACF49901.1, ECO:0000313|Proteomes:UP000001867}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R551-3 {ECO:0000313|EMBL:ACF49901.1,
RC   ECO:0000313|Proteomes:UP000001867};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L.,
RA   Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Taghavi S., Monchy S., Newman L., Vangronsveld J.,
RA   van der Lelie D., Richardson P.;
RT   "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001111; ACF49901.1; -; Genomic_DNA.
DR   RefSeq; WP_012509745.1; NC_011071.1.
DR   STRING; 391008.Smal_0196; -.
DR   EnsemblBacteria; ACF49901; ACF49901; Smal_0196.
DR   KEGG; smt:Smal_0196; -.
DR   eggNOG; ENOG4108JIK; Bacteria.
DR   eggNOG; COG4770; LUCA.
DR   HOGENOM; HOG000008989; -.
DR   KO; K01968; -.
DR   OMA; LVKWQLM; -.
DR   OrthoDB; 361205at2; -.
DR   BioCyc; SMAL391008:SMAL_RS00990-MONOMER; -.
DR   Proteomes; UP000001867; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
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   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; SSF51230; SSF51230; 1.
DR   SUPFAM; SSF51246; SSF51246; 1.
DR   SUPFAM; SSF52440; SSF52440; 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; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   4: Predicted;
DR   PRODOM; B4SSL9.
DR   SWISS-2DPAGE; B4SSL9.
KW   ATP-binding {ECO:0000256|PROSITE-ProRule:PRU00409,
KW   ECO:0000313|EMBL:ACF49901.1};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001867};
KW   Nucleotide-binding {ECO:0000256|PROSITE-ProRule:PRU00409}.
FT   DOMAIN        1    447       Biotin carboxylation.
FT                                {ECO:0000259|PROSITE:PS50979}.
FT   DOMAIN      120    317       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      578    658       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
SQ   SEQUENCE   660 AA;  70574 MW;  07D57EE2C1231A34 CRC64;
     MFTKVLIANR GEIACRVIAT CRRLGIATVA VYSDADRNAR HVRLADEAIH IGPAAARESY
     LRGDVLLDAA RRSGAQAIHP GYGFLSENAD FADACAAAGI TFIGPPASAI RAMGDKSAAK
     ALMAKAGVPL TPGYHGDQQA PDFLRAQADG IGYPVLIKAS AGGGGKGMRK VERSEDFVDA
     LASCQREAAS AFGNDHVLVE KYVERPRHIE IQVFGDSHGE AVYLFERDCS VQRRHQKVLE
     EAPAPGMSAE RRAAMGKAAV DAARAVGYVG AGTVEFIAGP DGDFYFMEMN TRLQVEHPVT
     EYITGTDLVE WQLRVASGQP LPLRQEQLAI HGHAIEARLY AEDADRGFLP STGTLRRLRL
     PMPSANVRVD TGVEEGDSIS PYYDPMIAKL IVWDVDRDAA LRRMSQALAD CQVVGVTTNA
     GFLRRLVNTD SFAHAKLDTA LIEREQAALS AAGDSDDALW QLAAVAAVAS TADAGIDARD
     PHSPWQAQDG WRLGASTPRA LPLQQGERTH TLKVWVQADG WRVQSDDAAP VQVIGTANAQ
     GLTVQLGERR WSLQLLREGD QLYLFGADGQ HRFTLHDPVG ESDTAVADAG SLLAPMPGKI
     VATLVAAGTE VKRGTPLVVL EAMKMEHTLQ APADGTVKGY RAKAGDQVGD GAVLVDFEAA
//

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