(data stored in ACNUC7421 zone)

SWISSPROT: C8W635_DESAS

ID   C8W635_DESAS            Unreviewed;       320 AA.
AC   C8W635;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 75.
DE   RecName: Full=Ornithine carbamoyltransferase {ECO:0000256|SAAS:SAAS00393033};
DE            EC=2.1.3.3 {ECO:0000256|SAAS:SAAS00393033};
GN   OrderedLocusNames=Dtox_0570 {ECO:0000313|EMBL:ACV61490.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61490.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61490.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group
CC       from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine
CC       (ORN) to produce L-citrulline. {ECO:0000256|SAAS:SAAS00009102}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline +
CC         phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743,
CC         ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_01109, ECO:0000256|SAAS:SAAS01125822};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
CC       ECO:0000256|SAAS:SAAS00341539}.
CC   -!- SIMILARITY: Belongs to the ATCase/OTCase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01109, ECO:0000256|RuleBase:RU003634,
CC       ECO:0000256|SAAS:SAAS00578869}.
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DR   EMBL; CP001720; ACV61490.1; -; Genomic_DNA.
DR   RefSeq; WP_015756209.1; NC_013216.1.
DR   STRING; 485916.Dtox_0570; -.
DR   EnsemblBacteria; ACV61490; ACV61490; Dtox_0570.
DR   KEGG; dae:Dtox_0570; -.
DR   eggNOG; ENOG4105DBV; Bacteria.
DR   eggNOG; COG0078; LUCA.
DR   HOGENOM; HOG000022686; -.
DR   KO; K00611; -.
DR   OMA; DGNNVCN; -.
DR   OrthoDB; 988597at2; -.
DR   BioCyc; DACE485916:G1GFV-577-MONOMER; -.
DR   Proteomes; UP000002217; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.1370; -; 2.
DR   HAMAP; MF_01109; OTCase; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024904; OTCase_ArgI.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; SSF53671; 1.
DR   TIGRFAMs; TIGR00658; orni_carb_tr; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8W635.
DR   SWISS-2DPAGE; C8W635.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|SAAS:SAAS00420337};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01109,
KW   ECO:0000256|RuleBase:RU003634, ECO:0000256|SAAS:SAAS00470455,
KW   ECO:0000313|EMBL:ACV61490.1}.
FT   DOMAIN       16    156       OTCace_N. {ECO:0000259|Pfam:PF02729}.
FT   DOMAIN      163    316       OTCace. {ECO:0000259|Pfam:PF00185}.
FT   REGION       65     68       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      143    146       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   REGION      242    243       Ornithine binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   REGION      278    279       Carbamoyl phosphate binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_01109}.
FT   COILED      300    320       {ECO:0000256|SAM:Coils}.
FT   BINDING      92     92       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     116    116       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
FT   BINDING     174    174       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     238    238       Ornithine. {ECO:0000256|HAMAP-Rule:
FT                                MF_01109}.
FT   BINDING     306    306       Carbamoyl phosphate. {ECO:0000256|HAMAP-
FT                                Rule:MF_01109}.
SQ   SEQUENCE   320 AA;  35424 MW;  FA3E806743990453 CRC64;
     MSSLLQLPIS KDFKGRDFLL LLDFSAEEIK HLINVAVELK AIQKKGEPHP YLQGKTLAMI
     FQKSSTRTRV SFEVAMYQLG GYPLFLSSND LQMGRGETIA DTARTLSRYV DGIMIRTYAQ
     SDVEELAEYA DIPVINGLTD LVHPTQVIAD LQTVLEHKGK LAGLKMAFLG DGNNVAHSLM
     AGCAKVGMNI TLANPAGYKP LPEMVEKAKQ VAETTGSIIE IIEDPVAAVK DADVIYTDVW
     ASMGQEKEQE ERAKMMAPYQ VNAELVRHAK PDYIFLHCLP AKREQEVTSE ILDSNHSAAF
     DEAENRLHAH KAILALLMQK
//

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