(data stored in SCRATCH zone)

SWISSPROT: A0LE60_SYNFM

ID   A0LE60_SYNFM            Unreviewed;      1080 AA.
AC   A0LE60;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 91.
DE   RecName: Full=Carbamoyl-phosphate synthase large chain {ECO:0000256|HAMAP-Rule:MF_01210};
DE            EC=6.3.5.5 {ECO:0000256|HAMAP-Rule:MF_01210};
DE   AltName: Full=Carbamoyl-phosphate synthetase ammonia chain {ECO:0000256|HAMAP-Rule:MF_01210};
GN   Name=carB {ECO:0000256|HAMAP-Rule:MF_01210};
GN   OrderedLocusNames=Sfum_0008 {ECO:0000313|EMBL:ABK15712.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK15712.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK15712.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP +
CC         carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate;
CC         Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:456216; EC=6.3.5.5; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01210, ECO:0000256|SAAS:SAAS01124510};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|SAAS:SAAS00981842};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|SAAS:SAAS00611658};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis;
CC       carbamoyl phosphate from bicarbonate: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00981844}.
CC   -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo
CC       pathway; (S)-dihydroorotate from bicarbonate: step 1/3.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS01000080}.
CC   -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain
CC       promotes the hydrolysis of glutamine to ammonia, which is used by
CC       the large (or ammonia) chain to synthesize carbamoyl phosphate.
CC       {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|SAAS:SAAS00570548}.
CC   -!- SIMILARITY: Belongs to the CarB family. {ECO:0000256|HAMAP-
CC       Rule:MF_01210, ECO:0000256|SAAS:SAAS00570556}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01210}.
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DR   EMBL; CP000478; ABK15712.1; -; Genomic_DNA.
DR   RefSeq; WP_011696885.1; NC_008554.1.
DR   STRING; 335543.Sfum_0008; -.
DR   EnsemblBacteria; ABK15712; ABK15712; Sfum_0008.
DR   KEGG; sfu:Sfum_0008; -.
DR   eggNOG; ENOG4105CU6; Bacteria.
DR   eggNOG; COG0458; LUCA.
DR   HOGENOM; HOG000234582; -.
DR   KO; K01955; -.
DR   OMA; AVFPFNK; -.
DR   OrthoDB; 48855at2; -.
DR   BioCyc; SFUM335543:G1G7I-10-MONOMER; -.
DR   UniPathway; UPA00068; UER00171.
DR   UniPathway; UPA00070; UER00115.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd01424; MGS_CPS_II; 1.
DR   Gene3D; 1.10.1030.10; -; 1.
DR   Gene3D; 3.40.50.1380; -; 1.
DR   HAMAP; MF_01210_A; CPSase_L_chain_A; 1.
DR   HAMAP; MF_01210_B; CPSase_L_chain_B; 1.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR006275; CarbamoylP_synth_lsu.
DR   InterPro; IPR005480; CarbamoylP_synth_lsu_oligo.
DR   InterPro; IPR036897; CarbamoylP_synth_lsu_oligo_sf.
DR   InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR   InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom.
DR   InterPro; IPR011607; MGS-like_dom.
DR   InterPro; IPR036914; MGS-like_dom_sf.
DR   InterPro; IPR033937; MGS_CPS_CarB.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   Pfam; PF02786; CPSase_L_D2; 2.
DR   Pfam; PF02787; CPSase_L_D3; 1.
DR   Pfam; PF02142; MGS; 1.
DR   PRINTS; PR00098; CPSASE.
DR   SMART; SM01096; CPSase_L_D3; 1.
DR   SMART; SM00851; MGS; 1.
DR   SUPFAM; SSF48108; SSF48108; 1.
DR   SUPFAM; SSF52335; SSF52335; 1.
DR   SUPFAM; SSF52440; SSF52440; 2.
DR   TIGRFAMs; TIGR01369; CPSaseII_lrg; 1.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00866; CPSASE_1; 2.
DR   PROSITE; PS00867; CPSASE_2; 2.
PE   3: Inferred from homology;
DR   PRODOM; A0LE60.
DR   SWISS-2DPAGE; A0LE60.
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981831};
KW   Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981841};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01210, ECO:0000256|PROSITE-
KW   ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710217};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Ligase {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00710245};
KW   Magnesium {ECO:0000256|SAAS:SAAS00981805};
KW   Manganese {ECO:0000256|SAAS:SAAS00459951};
KW   Metal-binding {ECO:0000256|SAAS:SAAS00086100};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|PROSITE-ProRule:PRU00409, ECO:0000256|SAAS:SAAS00710285};
KW   Pyrimidine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS01000143};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Repeat {ECO:0000256|HAMAP-Rule:MF_01210,
KW   ECO:0000256|SAAS:SAAS00981845}.
FT   DOMAIN      133    328       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   DOMAIN      680    871       ATP-grasp. {ECO:0000259|PROSITE:PS50975}.
FT   REGION        1    402       Carboxyphosphate synthetic domain.
FT                                {ECO:0000256|HAMAP-Rule:MF_01210}.
FT   REGION      938   1080       Allosteric domain. {ECO:0000256|HAMAP-
FT                                Rule:MF_01210}.
SQ   SEQUENCE   1080 AA;  119301 MW;  39D59D5DD1607DD0 CRC64;
     MPKRTDIRKI LIIGSGPIII SQACEFDYSG TQACKALREE GYEIVLINSN PATIMTDPET
     ADRTYIEPIT PEAVAKVIER ERPDALLPTL GGQTALNVAV RVAETGVLER FGVALIGASV
     EVIKKAEDRE LFRDAMKRIG LRVPASGIAR SMSEVESIAR EIGFPIIVRP SFTLGGTGGG
     VAYNREELKE LAQSGLDASF IHTVMLEESV LGWKEFELEV MRDCMDNVVI ICSIENMDAM
     GVHTGDSITV APAQTLTDRE YQLLRDASIA ILREIGVETG GSNVQFAINP ADGEMVVIEM
     NPRVSRSSAL ASKATGFPIA KIAAKLAVGY SLDEIANDIT RETRASFEPT IDYCVVKVPR
     FTFEKFPRTE DFLSTSMKSV GETMAIGRTF KEALHKAVRS LEIGRFGFVD PPANADREYM
     ERLRQKLRRP NSMRLFQIGE ALKLGMPIEE LHALTFIDPW FLHHIRQVLL LEDEIRGDAD
     RSGFLDDPER VRYAKSWGFS DVRLAQLSGS DEETVRQLRI KHGIKPVYKL VDTCAAEFEA
     YTPYYYSTYE TEDEARPTGR PKVVILGGGP NRIGQGIEFD YCCVHASFSL REEDHESIMV
     NSNPETVSTD YDTSDKLYFE PLTREDVLHI LDTEKPKGVI VQFGGQTPLN LSVPLEKAGA
     RILGTSPDAI DRAEDRKRFQ KLLQKLGLKQ PRNATAFTLR EAAEAAGRIG YPVVVRPSYV
     LGGRAMEIVF DAAMLESFMK TAVHVSPGHP ILIDQFLEDA VEIDVDAISD GTVTVVGGIM
     EHIEQAGIHS GDSACVLPPM SISRSIQEEI RRQTRLLAKE LGVVGLMNIQ FALQNGEIFI
     LEVNPRASRT IPFVSKAIGF PLAKLATRVM LGKSLKELGF DTEVEPEHIS VKEAVFPFSR
     FPNVDVLLGP EMKSTGEVMG IGSTFGIAFA KAQAAVGYEL PTSGTVFISV HDADKPKVLS
     VARKFGEMGF QLIATAGTAD FLNGNGIRTR PVFKLKEGRP HVVDRIKNGE VQLVVNTSMG
     KKTTSDSYEI RRTTLIYNIP YATTIAGAKA MAEAVSELQR GDWDVRTLQE YHHRERSRRQ
//

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