SOTC_BACTN
ID SOTC_BACTN Reviewed; 318 AA.
AC Q8A1E9;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=N-succinylornithine carbamoyltransferase {ECO:0000250|UniProtKB:E1WKT5};
DE EC=2.1.3.11 {ECO:0000250|UniProtKB:E1WKT5};
DE AltName: Full=N-succinyl-L-ornithine transcarbamylase {ECO:0000255|HAMAP-Rule:MF_02235};
DE Short=SOTCase {ECO:0000255|HAMAP-Rule:MF_02235};
GN Name=argF' {ECO:0000255|HAMAP-Rule:MF_02235}; OrderedLocusNames=BT_3717;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
CC -!- FUNCTION: Catalyzes the transfer of the carbamoyl group from carbamoyl
CC phosphate to the delta-amino group of N(2)-succinyl-L-ornithine to
CC produce N(2)-succinyl-L-citrulline. Is essential for arginine
CC biosynthesis. Has no activity with either L-ornithine or L-aspartate as
CC substrate. Has also no detectable AOTCase activity, being unable to
CC convert N(2)-acetyl-L-ornithine to N(2)-acetyl-L-citrulline.
CC {ECO:0000250|UniProtKB:E1WKT5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + N(2)-succinyl-L-ornithine = H(+) + N(2)-
CC succinyl-L-citrulline + phosphate; Xref=Rhea:RHEA:25884,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228,
CC ChEBI:CHEBI:58514, ChEBI:CHEBI:58862; EC=2.1.3.11;
CC Evidence={ECO:0000250|UniProtKB:E1WKT5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25885;
CC Evidence={ECO:0000250|UniProtKB:E1WKT5};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000250|UniProtKB:E1WKT5}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:E1WKT5}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. SOTCase family. {ECO:0000255|HAMAP-Rule:MF_02235,
CC ECO:0000305}.
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DR EMBL; AE015928; AAO78822.1; -; Genomic_DNA.
DR RefSeq; NP_812628.1; NC_004663.1.
DR RefSeq; WP_008762653.1; NZ_UYXG01000004.1.
DR AlphaFoldDB; Q8A1E9; -.
DR SMR; Q8A1E9; -.
DR STRING; 226186.BT_3717; -.
DR PaxDb; Q8A1E9; -.
DR PRIDE; Q8A1E9; -.
DR EnsemblBacteria; AAO78822; AAO78822; BT_3717.
DR GeneID; 60924886; -.
DR KEGG; bth:BT_3717; -.
DR PATRIC; fig|226186.12.peg.3778; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_3_10; -.
DR InParanoid; Q8A1E9; -.
DR OMA; VYVKNWS; -.
DR BioCyc; MetaCyc:MON-14262; -.
DR BRENDA; 2.1.3.11; 755.
DR UniPathway; UPA00068; -.
DR EvolutionaryTrace; Q8A1E9; -.
DR Proteomes; UP000001414; Chromosome.
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:0019240; P:citrulline biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_02235; SOTCase; 1.
DR InterPro; IPR043696; ArgF'-like.
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 Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR SUPFAM; SSF53671; SSF53671; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Reference proteome;
KW Transferase.
FT CHAIN 1..318
FT /note="N-succinylornithine carbamoyltransferase"
FT /id="PRO_0000113266"
FT BINDING 47..50
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 75
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 110
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 142
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 147..150
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 176
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 236
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 274..275
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 278
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT BINDING 302
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
FT SITE 90
FT /note="Key residue in conferring substrate specificity for
FT N-succinyl-L-ornithine versus N-acetyl-L-ornithine"
FT /evidence="ECO:0000250|UniProtKB:E1WKT5"
SQ SEQUENCE 318 AA; 36383 MW; 88116898BD42822B CRC64;
MKKFTCVQDI GDLKSALAEA FEIQKDRFKY VELGRNKTLM MIFFNSSLRT RLSTQKAALN
LGMNVMVLDI NQGAWKLETE RGVIMDGDKP EHLLEAIPVM GCYCDIIGVR SFARFEDRDF
DYQETILNQF IQYSGRPVFS MEAATRHPLQ SFADLITIEE YKKTARPKVV MTWAPHPRPL
PQAVPNSFAE WMNATDYDFV ITHPEGYELA PQFVGNAKVE YDQMKAFEGA DFIYAKNWAA
YTGDNYGQIL SKDREWTVSD RQMAVTNNAF FMHCLPVRRN MIVTDDVIES PQSIVIPEAA
NREISATVVL KRLIEGLE
