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Database: UniProt
Entry: Q1GSX6_SPHAL
LinkDB: Q1GSX6_SPHAL
Original site: Q1GSX6_SPHAL 
ID   Q1GSX6_SPHAL            Unreviewed;       612 AA.
AC   Q1GSX6;
DT   27-JUN-2006, integrated into UniProtKB/TrEMBL.
DT   27-JUN-2006, sequence version 1.
DT   24-JAN-2024, entry version 105.
DE   SubName: Full=Carbamoyl-phosphate synthase L chain, ATP-binding {ECO:0000313|EMBL:ABF53246.1};
GN   OrderedLocusNames=Sala_1533 {ECO:0000313|EMBL:ABF53246.1};
OS   Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256)
OS   (Sphingomonas alaskensis).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingopyxis.
OX   NCBI_TaxID=317655 {ECO:0000313|EMBL:ABF53246.1, ECO:0000313|Proteomes:UP000006578};
RN   [1] {ECO:0000313|EMBL:ABF53246.1, ECO:0000313|Proteomes:UP000006578}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13593 / LMG 18877 / RB2256
RC   {ECO:0000313|Proteomes:UP000006578};
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586;
CC         Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR   EMBL; CP000356; ABF53246.1; -; Genomic_DNA.
DR   RefSeq; WP_011541826.1; NC_008048.1.
DR   AlphaFoldDB; Q1GSX6; -.
DR   STRING; 317655.Sala_1533; -.
DR   KEGG; sal:Sala_1533; -.
DR   eggNOG; COG4770; Bacteria.
DR   HOGENOM; CLU_000395_3_1_5; -.
DR   OMA; YFPRVRH; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000006578; 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:UP000006578}.
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          532..609
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   612 AA;  64761 MW;  A99A018E4F8CEE1B CRC64;
     MIQSLLIANR GEIACRIIRT AREMGIRTVA VYSDADAKAL HVRQADEAVH IGPSPARESY
     LVGEKIVAAA KATGAEAIHP GYGFLSENAA FAQAVIDAGL VWVGPNPASI TAMGLKDAAK
     KLMAEAGVPV TPGYMGENQD PAFLAERAAE IGYPVLIKAV AGGGGKGMRK VDSPADFLDA
     LASCQREAAA SFGNDHVLIE KYILTPRHIE VQIFGDTHGN VVHLFERDCS LQRRHQKVIE
     EAPAPGMDEA TRAELCAAAV RAAKAVDYVG AGTIEFIADA SEGLRADRIW FMEMNTRLQV
     EHPVTEEITG VDLVEWQLRV ASGEPLPLTQ DQLAINGWAM EARLYAEDPA KGFLPSTGTL
     ELFQLPEHIG RIDTGVYEGA EVSPFYDPMI AKVIAYGENR EEARELLSEM LEDSAIWPVK
     TNSAFLIAAL DHPDFVAGTV DTGLIGRDGD AMTAAPEPSA QALTNAAMAM VPRALQAGFR
     LNAPEVRTAP FLLDGKRVDV ALHGPGAEEP APAMLVAEGG SVWQLAPWRA EGSASGAAGD
     GAILSPMPGK IIAVEVAAGD TVAKGQKLLT LEAMKMEHSL VAPFDGVVAE LNAVAGGQVQ
     VEALLARIEA AK
//
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