OTC_BACAN
ID OTC_BACAN Reviewed; 316 AA.
AC Q81M99; Q6HTQ2; Q6KMZ0;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Ornithine carbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01109};
DE Short=OTCase {ECO:0000255|HAMAP-Rule:MF_01109};
DE EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN Name=argF {ECO:0000255|HAMAP-Rule:MF_01109};
GN OrderedLocusNames=BA_4351, GBAA_4351, BAS4036;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP X-RAY CRYSTALLOGRAPHY (3.25 ANGSTROMS).
RG Center for structural genomics of infectious diseases (CSGID);
RA Shabalin I.G., Mikolajczak K., Stam J., Winsor J., Shuvalova L.,
RA Anderson W.F., Minor W.;
RT "Crystal structure of anabolic ornithine carbamoyltransferase from Bacillus
RT anthracis.";
RL Submitted (APR-2012) to the PDB data bank.
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) IN COMPLEX WITH CARBAMOYL PHOSPHATE
RP AND SUBSTRATE ANALOG, AND SUBUNIT.
RA Shabalin I.G., Handing K., Cymborowski M.T., Stam J., Winsor J.,
RA Shuvalova L., Anderson W.F., Minor W.;
RT "Crystal structures and kinetic properties of anabolic ornithine
RT carbamoyltransferase from human pathogens Vibrio vulnificus and Bacillus
RT anthracis.";
RL Submitted (OCT-2013) to the PDB data bank.
CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC produce L-citrulline. {ECO:0000255|HAMAP-Rule:MF_01109}.
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:0000255|HAMAP-
CC Rule:MF_01109};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000255|HAMAP-
CC Rule:MF_01109}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000305|Ref.5}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01109}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000255|HAMAP-Rule:MF_01109}.
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DR EMBL; AE016879; AAP28069.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33470.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56337.1; -; Genomic_DNA.
DR RefSeq; NP_846583.1; NC_003997.3.
DR RefSeq; WP_000108878.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030286.1; NC_005945.1.
DR PDB; 4EP1; X-ray; 3.25 A; A/B=1-316.
DR PDB; 4NF2; X-ray; 1.74 A; A/B/C=1-316.
DR PDBsum; 4EP1; -.
DR PDBsum; 4NF2; -.
DR AlphaFoldDB; Q81M99; -.
DR SMR; Q81M99; -.
DR IntAct; Q81M99; 1.
DR STRING; 260799.BAS4036; -.
DR DNASU; 1087574; -.
DR EnsemblBacteria; AAP28069; AAP28069; BA_4351.
DR EnsemblBacteria; AAT33470; AAT33470; GBAA_4351.
DR GeneID; 45024016; -.
DR KEGG; ban:BA_4351; -.
DR KEGG; bar:GBAA_4351; -.
DR KEGG; bat:BAS4036; -.
DR PATRIC; fig|198094.11.peg.4319; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_2_9; -.
DR OMA; VYVKNWS; -.
DR UniPathway; UPA00068; UER00112.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; 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 GO; GO:0006526; P:arginine biosynthetic process; 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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Reference proteome; Transferase.
FT CHAIN 1..316
FT /note="Ornithine carbamoyltransferase"
FT /id="PRO_0000112875"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 166
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 230
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 234..235
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 269..270
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT BINDING 297
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PDB:4NF2"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 22..37
FT /evidence="ECO:0007829|PDB:4NF2"
FT TURN 43..46
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 59..70
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 74..79
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 80..82
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 84..87
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:4NF2"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 112..121
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 126..129
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 136..150
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 157..162
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 194..207
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 217..221
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 225..229
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 241..247
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:4NF2"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:4NF2"
FT TURN 275..277
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 280..283
FT /evidence="ECO:0007829|PDB:4NF2"
FT HELIX 290..310
FT /evidence="ECO:0007829|PDB:4NF2"
SQ SEQUENCE 316 AA; 35305 MW; E97F98B542E5EB7E CRC64;
MSTVQVPKLN TKDLLTLEEL TQEEIISLIE FAIYLKKNKQ EPLLQGKILG LIFDKHSTRT
RVSFEAGMVQ LGGHGMFLNG KEMQMGRGET VSDTAKVLSH YIDGIMIRTF SHADVEELAK
ESSIPVINGL TDDHHPCQAL ADLMTIYEET NTFKGIKLAY VGDGNNVCHS LLLASAKVGM
HMTVATPVGY KPNEEIVKKA LAIAKETGAE IEILHNPELA VNEADFIYTD VWMSMGQEGE
EEKYTLFQPY QINKELVKHA KQTYHFLHCL PAHREEEVTG EIIDGPQSIV FEQAGNRLHA
QKALLVSLFK NVEELS
