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
//