OTCC_SALTY
ID OTCC_SALTY Reviewed; 334 AA.
AC Q8ZK35;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Ornithine carbamoyltransferase, catabolic;
DE Short=OTCase;
DE EC=2.1.3.3;
GN Name=arcB; OrderedLocusNames=STM4465;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
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:0000250}.
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 -!- PATHWAY: Amino-acid degradation; L-arginine degradation via ADI
CC pathway; carbamoyl phosphate from L-arginine: step 2/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. OTCase family. {ECO:0000305}.
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DR EMBL; AE006468; AAL23284.1; -; Genomic_DNA.
DR RefSeq; NP_463325.1; NC_003197.2.
DR RefSeq; WP_000237031.1; NC_003197.2.
DR AlphaFoldDB; Q8ZK35; -.
DR SMR; Q8ZK35; -.
DR STRING; 99287.STM4465; -.
DR PaxDb; Q8ZK35; -.
DR EnsemblBacteria; AAL23284; AAL23284; STM4465.
DR GeneID; 1255991; -.
DR KEGG; stm:STM4465; -.
DR PATRIC; fig|99287.12.peg.4698; -.
DR HOGENOM; CLU_043846_3_1_6; -.
DR OMA; VYVKNWS; -.
DR PhylomeDB; Q8ZK35; -.
DR BioCyc; SENT99287:STM4465-MON; -.
DR UniPathway; UPA00254; UER00365.
DR Proteomes; UP000001014; 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; 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: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 3: Inferred from homology;
KW Arginine metabolism; Cytoplasm; Reference proteome; Transferase.
FT CHAIN 1..334
FT /note="Ornithine carbamoyltransferase, catabolic"
FT /id="PRO_0000113005"
FT BINDING 57..60
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 84
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 108
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 135..138
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 169
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 233
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 237..238
FT /ligand="L-ornithine"
FT /ligand_id="ChEBI:CHEBI:46911"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 275..276
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT BINDING 320
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
SQ SEQUENCE 334 AA; 36816 MW; 20C36699FC43C1C8 CRC64;
MVISLKNRNF LKLLDYTPAE IQHLIDLAIE LKAAKKAGCE KQTLIGKNIA LIFEKTSTRT
RCAFEVAAFD QGAQVTYLGP SGSQIGHKES MKDTARVLGR MYDGIEYRGF GQHIVEELGE
YAGVPVWNGL TDEFHPTQIL ADLMTMLEHA PGKTLPELSF AYLGDARNNM GNSLMVGAAK
MGMDIRLIAP KSFWPDAALV AQCREIASVT GARITLTESV EDGVHGVDFL YTDVWVSMGE
PKEAWAERVS LMTPYQVNQQ VVNATGNPDV KFMHCLPAFH NEHTKVGREI EMAYGLKGLE
VTEEVFESAG SIVFDEAENR MHTIKAVMVA TLGD
