SOTC_BACF6
ID SOTC_BACF6 Reviewed; 318 AA.
AC E1WKT5;
DT 18-SEP-2019, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=N-succinylornithine carbamoyltransferase {ECO:0000305|PubMed:16704984};
DE EC=2.1.3.11 {ECO:0000269|PubMed:16704984};
DE AltName: Full=N-succinyl-L-ornithine transcarbamylase {ECO:0000303|PubMed:16704984};
DE Short=SOTCase {ECO:0000303|PubMed:16704984};
GN Name=argF' {ECO:0000303|PubMed:16585758, ECO:0000303|PubMed:16704984};
GN Synonyms=argF {ECO:0000312|EMBL:CBW21098.1};
GN OrderedLocusNames=BF638R_0504 {ECO:0000312|EMBL:CBW21098.1};
OS Bacteroides fragilis (strain 638R).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=862962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=638R;
RX PubMed=20829291; DOI=10.1099/mic.0.042978-0;
RA Patrick S., Blakely G.W., Houston S., Moore J., Abratt V.R., Bertalan M.,
RA Cerdeno-Tarraga A.M., Quail M.A., Corton N., Corton C., Bignell A.,
RA Barron A., Clark L., Bentley S.D., Parkhill J.;
RT "Twenty-eight divergent polysaccharide loci specifying within- and amongst-
RT strain capsule diversity in three strains of Bacteroides fragilis.";
RL Microbiology 156:3255-3269(2010).
RN [2]
RP LACK OF AOTCASE ACTIVITY.
RC STRAIN=638R / TM 4000;
RX PubMed=16585758; DOI=10.1128/jb.188.8.2974-2982.2006;
RA Morizono H., Cabrera-Luque J., Shi D., Gallegos R., Yamaguchi S., Yu X.,
RA Allewell N.M., Malamy M.H., Tuchman M.;
RT "Acetylornithine transcarbamylase: a novel enzyme in arginine
RT biosynthesis.";
RL J. Bacteriol. 188:2974-2982(2006).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1-318, FUNCTION, PATHWAY,
RP DISRUPTION PHENOTYPE, AND SUBUNIT.
RC STRAIN=638R / TM 4000;
RX PubMed=12095263; DOI=10.1016/s0022-2836(02)00539-9;
RA Shi D., Gallegos R., DePonte J. III, Morizono H., Yu X., Allewell N.M.,
RA Malamy M., Tuchman M.;
RT "Crystal structure of a transcarbamylase-like protein from the anaerobic
RT bacterium Bacteroides fragilis at 2.0 A resolution.";
RL J. Mol. Biol. 320:899-908(2002).
RN [4] {ECO:0007744|PDB:2FG6, ECO:0007744|PDB:2FG7}
RP X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) IN COMPLEXES WITH
RP N-SUCCINYL-L-NORVALINE AND CARBAMOYL PHOSPHATE, FUNCTION, CATALYTIC
RP ACTIVITY, SUBSTRATE SPECIFICITY, PATHWAY, MUTAGENESIS OF PRO-90, AND
RP REACTION MECHANISM.
RC STRAIN=638R / TM 4000;
RX PubMed=16704984; DOI=10.1074/jbc.m601229200;
RA Shi D., Morizono H., Cabrera-Luque J., Yu X., Roth L., Malamy M.H.,
RA Allewell N.M., Tuchman M.;
RT "Structure and catalytic mechanism of a novel N-succinyl-L-ornithine
RT transcarbamylase in arginine biosynthesis of Bacteroides fragilis.";
RL J. Biol. Chem. 281:20623-20631(2006).
RN [5] {ECO:0007744|PDB:2G7M}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF MUTANT GLU-90 IN COMPLEX WITH
RP CARBAMOYL PHOSPHATE AND N-ACETYLNORVALINE.
RX PubMed=17600144; DOI=10.1110/ps.072919907;
RA Shi D., Yu X., Cabrera-Luque J., Chen T.Y., Roth L., Morizono H.,
RA Allewell N.M., Tuchman M.;
RT "A single mutation in the active site swaps the substrate specificity of N-
RT acetyl-L-ornithine transcarbamylase and N-succinyl-L-ornithine
RT transcarbamylase.";
RL Protein Sci. 16:1689-1699(2007).
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 (PubMed:16704984). Is essential for
CC arginine biosynthesis (PubMed:12095263, PubMed:16704984). Has no
CC activity with either L-ornithine or L-aspartate as substrate
CC (PubMed:12095263, PubMed:16704984). Has also no detectable AOTCase
CC activity, being unable to convert N(2)-acetyl-L-ornithine to N(2)-
CC acetyl-L-citrulline (PubMed:16585758, PubMed:16704984).
CC {ECO:0000269|PubMed:12095263, ECO:0000269|PubMed:16585758,
CC ECO:0000269|PubMed:16704984, ECO:0000303|PubMed:12095263}.
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:0000269|PubMed:16704984};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25885;
CC Evidence={ECO:0000269|PubMed:16704984};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000269|PubMed:12095263, ECO:0000269|PubMed:16704984}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12095263}.
CC -!- DISRUPTION PHENOTYPE: Disruption of this gene results in mutants that
CC require exogenous arginine for growth. {ECO:0000303|PubMed:12095263}.
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; FQ312004; CBW21098.1; -; Genomic_DNA.
DR RefSeq; WP_005796520.1; NC_016776.1.
DR PDB; 1JS1; X-ray; 2.00 A; X/Y/Z=1-318.
DR PDB; 2FG6; X-ray; 2.80 A; C/D/E/X/Y/Z=1-318.
DR PDB; 2FG7; X-ray; 2.90 A; C/D/E/X/Y/Z=1-318.
DR PDB; 2G7M; X-ray; 2.90 A; C/D/E/X/Y/Z=1-318.
DR PDBsum; 1JS1; -.
DR PDBsum; 2FG6; -.
DR PDBsum; 2FG7; -.
DR PDBsum; 2G7M; -.
DR AlphaFoldDB; E1WKT5; -.
DR SMR; E1WKT5; -.
DR PRIDE; E1WKT5; -.
DR EnsemblBacteria; CBW21098; CBW21098; BF638R_0504.
DR GeneID; 66330457; -.
DR KEGG; bfg:BF638R_0504; -.
DR PATRIC; fig|862962.3.peg.520; -.
DR HOGENOM; CLU_043846_3_3_10; -.
DR OMA; VYVKNWS; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000008560; Chromosome.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IEA:InterPro.
DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-UniRule.
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 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Transferase.
FT CHAIN 1..318
FT /note="N-succinylornithine carbamoyltransferase"
FT /id="PRO_0000447708"
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:0000269|PubMed:16704984,
FT ECO:0000269|PubMed:17600144, ECO:0007744|PDB:2FG7,
FT ECO:0007744|PDB:2G7M"
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:0000269|PubMed:16704984,
FT ECO:0000269|PubMed:17600144, ECO:0007744|PDB:2FG7,
FT ECO:0007744|PDB:2G7M"
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:0000269|PubMed:16704984,
FT ECO:0000269|PubMed:17600144, ECO:0007744|PDB:2FG7,
FT ECO:0007744|PDB:2G7M"
FT BINDING 142
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000305|PubMed:16704984,
FT ECO:0000305|PubMed:17600144, ECO:0007744|PDB:2FG6,
FT ECO:0007744|PDB:2FG7"
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:0000269|PubMed:16704984,
FT ECO:0000269|PubMed:17600144, ECO:0007744|PDB:2FG7,
FT ECO:0007744|PDB:2G7M"
FT BINDING 176
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000305|PubMed:16704984,
FT ECO:0007744|PDB:2FG6, ECO:0007744|PDB:2FG7"
FT BINDING 236
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000305|PubMed:16704984,
FT ECO:0000305|PubMed:17600144, ECO:0007744|PDB:2FG6,
FT ECO:0007744|PDB:2FG7"
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:0000269|PubMed:16704984,
FT ECO:0000269|PubMed:17600144, ECO:0007744|PDB:2FG7,
FT ECO:0007744|PDB:2G7M"
FT BINDING 278
FT /ligand="N(2)-succinyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:58514"
FT /evidence="ECO:0000305|PubMed:16704984,
FT ECO:0007744|PDB:2FG6, ECO:0007744|PDB:2FG7"
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:0000269|PubMed:16704984,
FT ECO:0000269|PubMed:17600144, ECO:0007744|PDB:2FG7,
FT ECO:0007744|PDB:2G7M"
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:0000269|PubMed:16704984"
FT MUTAGEN 90
FT /note="P->E: Generates an enzyme capable of carbamoylation
FT of N-acetyl-L-ornithine at a rate 7-times greater than N-
FT succinyl-L-ornithine, thus practically converting it from a
FT N-succinylornithine transcarbamylase (SOTCase) to a N-
FT acetylornithine transcarbamylase (AOTCase)."
FT /evidence="ECO:0000269|PubMed:16704984"
SQ SEQUENCE 318 AA; 36405 MW; 930ECC6E31C5916F CRC64;
MKKFTCVQDI GDLKSALAES FEIKKDRFKY VELGRNKTLL MIFFNSSLRT RLSTQKAALN
LGMNVIVLDI NQGAWKLETE RGVIMDGDKP EHLLEAIPVM GCYCDIIGVR SFARFENREY
DYNEVIINQF IQHSGRPVFS MEAATRHPLQ SFADLITIEE YKKTARPKVV MTWAPHPRPL
PQAVPNSFAE WMNATDYEFV ITHPEGYELD PKFVGNARVE YDQMKAFEGA DFIYAKNWAA
YTGDNYGQIL STDRNWTVGD RQMAVTNNAY FMHCLPVRRN MIVTDDVIES PQSIVIPEAA
NREISATVVL KRLLENLP
