OTCC_HALSA
ID OTCC_HALSA Reviewed; 295 AA.
AC Q48296; Q59454; Q9HHN0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic;
DE Short=cOTCase;
DE EC=2.1.3.3;
GN Name=arcB; Synonyms=argB; OrderedLocusNames=VNG_6315G;
OS Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
OS (Halobacterium halobium).
OG Plasmid pNRC200.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Halobacteriaceae; Halobacterium.
OX NCBI_TaxID=64091;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION AS A
RP COTCASE, BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=R1 / S9 / L33;
RX PubMed=7868583; DOI=10.1128/jb.177.5.1129-1136.1995;
RA Ruepp A., Mueller H., Lottspeich F., Soppa J.;
RT "Catabolic ornithine transcarbamylase of Halobacterium halobium
RT (salinarium): purification, characterization, sequence determination, and
RT evolution.";
RL J. Bacteriol. 177:1129-1136(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=R1 / S9 / L33;
RX PubMed=8759859; DOI=10.1128/jb.178.16.4942-4947.1996;
RA Ruepp A., Soppa J.;
RT "Fermentative arginine degradation in Halobacterium salinarium (formerly
RT Halobacterium halobium): genes, gene products, and transcripts of the
RT arcRACB gene cluster.";
RL J. Bacteriol. 178:4942-4947(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700922 / JCM 11081 / NRC-1; PLASMID=pNRC200;
RX PubMed=11016950; DOI=10.1073/pnas.190337797;
RA Ng W.V., Kennedy S.P., Mahairas G.G., Berquist B., Pan M., Shukla H.D.,
RA Lasky S.R., Baliga N.S., Thorsson V., Sbrogna J., Swartzell S., Weir D.,
RA Hall J., Dahl T.A., Welti R., Goo Y.A., Leithauser B., Keller K., Cruz R.,
RA Danson M.J., Hough D.W., Maddocks D.G., Jablonski P.E., Krebs M.P.,
RA Angevine C.M., Dale H., Isenbarger T.A., Peck R.F., Pohlschroder M.,
RA Spudich J.L., Jung K.-H., Alam M., Freitas T., Hou S., Daniels C.J.,
RA Dennis P.P., Omer A.D., Ebhardt H., Lowe T.M., Liang P., Riley M., Hood L.,
RA DasSarma S.;
RT "Genome sequence of Halobacterium species NRC-1.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:12176-12181(2000).
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:0000269|PubMed:7868583}.
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;
CC -!- ACTIVITY REGULATION: Arginine lead to a slight activation. Inhibited by
CC all nucleotide phosphates. {ECO:0000269|PubMed:7868583}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 mM for carbamoyl phosphate {ECO:0000269|PubMed:7868583};
CC KM=8 mM for L-ornithine {ECO:0000269|PubMed:7868583};
CC pH dependence:
CC Optimum pH is 8.8. At the physiological pH of 7, activity is only
CC about 30%. {ECO:0000269|PubMed:7868583};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:7868583}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- MISCELLANEOUS: Not stable below 1 M KCl. {ECO:0000305|PubMed:7868583}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; X81712; CAA57356.1; -; Genomic_DNA.
DR EMBL; X80931; CAA56906.1; -; Genomic_DNA.
DR EMBL; AE004438; AAG20946.1; -; Genomic_DNA.
DR PIR; S49261; S49261.
DR RefSeq; WP_010904159.1; NZ_BK010831.1.
DR AlphaFoldDB; Q48296; -.
DR SMR; Q48296; -.
DR EnsemblBacteria; AAG20946; AAG20946; VNG_6315G.
DR GeneID; 5954933; -.
DR GeneID; 62888214; -.
DR KEGG; hal:VNG_6315G; -.
DR PATRIC; fig|64091.14.peg.2292; -.
DR HOGENOM; CLU_043846_3_2_2; -.
DR InParanoid; Q48296; -.
DR OMA; DGNNVCN; -.
DR OrthoDB; 43727at2157; -.
DR PhylomeDB; Q48296; -.
DR BioCyc; MetaCyc:MON-662; -.
DR BRENDA; 2.1.3.3; 2552.
DR UniPathway; UPA00254; UER00365.
DR Proteomes; UP000000554; Plasmid pNRC200.
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; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR GO; GO:0019547; P:arginine catabolic process to ornithine; IEA:UniProtKB-UniPathway.
DR GO; GO:0019546; P:arginine deiminase pathway; IEA:UniProtKB-UniRule.
DR GO; GO:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
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 Arginine metabolism; Cytoplasm; Direct protein sequencing; Plasmid;
KW Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000113063"
FT BINDING 49..52
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 76
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 100
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 127..130
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 155
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 213
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 217..218
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 253..254
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 281
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ SEQUENCE 295 AA; 32676 MW; BFF6E002AC0289A2 CRC64;
MEHLVDINDV ESEEIEQLLD LAASMKENPG EFSGVMDNKS LVMLFAKPST RTRLSFETGM
TQLGGHGIFF EMGSSQLSRG EPISDVSQVM SRYEDAIMAR LFEHDEMMEL AENADVPVVN
GLTDFLHPCQ ALTDMFTMQE KDRLDTLAFV GDGNNVAHSL MQASAKMGVD CRIATPEGME
PDEEIQDRVS DANVTVTNDP YEAVDGATAV YGDVFVSMGE EEQREEKLAE FDGFQIDQDL
MDAARDDAIF MHCLPAHRGE EVTAEVADGP QSVIFDQAEN RMHVQKAIVH TLVNQ
