AOTC_XANAC
ID AOTC_XANAC Reviewed; 343 AA.
AC Q8PK25;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=N-acetylornithine carbamoyltransferase {ECO:0000250|UniProtKB:Q8P8J2};
DE EC=2.1.3.9 {ECO:0000250|UniProtKB:Q8P8J2};
DE AltName: Full=N-acetyl-L-ornithine transcarbamylase {ECO:0000255|HAMAP-Rule:MF_02234};
DE Short=AOTCase {ECO:0000255|HAMAP-Rule:MF_02234};
DE Short=Acetylornithine transcarbamylase {ECO:0000255|HAMAP-Rule:MF_02234};
GN Name=argF' {ECO:0000255|HAMAP-Rule:MF_02234}; OrderedLocusNames=XAC2352;
OS Xanthomonas axonopodis pv. citri (strain 306).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=190486;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=306;
RX PubMed=12024217; DOI=10.1038/417459a;
RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R.,
RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr.,
RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G.,
RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B.,
RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B.,
RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F.,
RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T.,
RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A.,
RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J.,
RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M.,
RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A.,
RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A.,
RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M.,
RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.;
RT "Comparison of the genomes of two Xanthomonas pathogens with differing host
RT specificities.";
RL Nature 417:459-463(2002).
CC -!- FUNCTION: Catalyzes the transfer of the carbamoyl group from carbamoyl
CC phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to
CC produce N(2)-acetyl-L-citrulline. This is a step in an alternative
CC arginine biosynthesis pathway. The enzyme has no activity with
CC ornithine. {ECO:0000250|UniProtKB:Q8P8J2}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=carbamoyl phosphate + N(2)-acetyl-L-ornithine = H(+) + N(2)-
CC acetyl-L-citrulline + phosphate; Xref=Rhea:RHEA:18609,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57805,
CC ChEBI:CHEBI:58228, ChEBI:CHEBI:58765; EC=2.1.3.9;
CC Evidence={ECO:0000250|UniProtKB:Q8P8J2};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18610;
CC Evidence={ECO:0000250|UniProtKB:Q8P8J2};
CC -!- ACTIVITY REGULATION: Carboxylation at Lys-302 increases the catalytic
CC activity of the enzyme. {ECO:0000250|UniProtKB:Q8P8J2}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000250|UniProtKB:Q8P8J2}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:Q8P8J2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. AOTCase family. {ECO:0000255|HAMAP-Rule:MF_02234,
CC ECO:0000305}.
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DR EMBL; AE008923; AAM37204.1; -; Genomic_DNA.
DR RefSeq; WP_003486947.1; NC_003919.1.
DR AlphaFoldDB; Q8PK25; -.
DR SMR; Q8PK25; -.
DR STRING; 190486.XAC2352; -.
DR EnsemblBacteria; AAM37204; AAM37204; XAC2352.
DR GeneID; 66911471; -.
DR KEGG; xac:XAC2352; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_3_6; -.
DR OMA; VYVKNWS; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000000576; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR GO; GO:0043857; F:N-acetylornithine carbamoyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR Gene3D; 3.40.50.1370; -; 2.
DR HAMAP; MF_02234; AOTCase; 1.
DR InterPro; IPR043695; ArgF.
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; Cytoplasm; Transferase.
FT CHAIN 1..343
FT /note="N-acetylornithine carbamoyltransferase"
FT /id="PRO_0000113267"
FT BINDING 49..52
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:Q8P8J2"
FT BINDING 77
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:Q8P8J2"
FT BINDING 112
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:Q8P8J2"
FT BINDING 144
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000250|UniProtKB:Q8P8J2"
FT BINDING 148..151
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:Q8P8J2"
FT BINDING 252
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000250|UniProtKB:Q8P8J2"
FT BINDING 294..295
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:Q8P8J2"
FT BINDING 295
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000250|UniProtKB:Q8P8J2"
FT BINDING 322
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:Q8P8J2"
FT SITE 92
FT /note="Key residue in conferring substrate specificity for
FT N-acetyl-L-ornithine versus N-succinyl-L-ornithine"
FT /evidence="ECO:0000250|UniProtKB:Q8P8J2"
FT MOD_RES 302
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000250|UniProtKB:Q8P8J2"
SQ SEQUENCE 343 AA; 38291 MW; CA7C7E3B5D50F563 CRC64;
MSLKHFLNTQ DWSRAELDAL LTQAALFKRN KLGSELKGKS IALVFFNPSM RTRTSFELGA
FQLGGHAVVL QPGKDAWPIE FNLGTVMDGD TEEHIAEVAR VLGRYVDLIG VRAFPKFVDW
SKDREDQVLK SFAKYSPVPV INMETITHPC QELAHALALQ EHFGTQDLRG KKYVLTWTYH
PKPLNTAVAN SALTIATRMG MDVTLLCPTP DYILDQRYMD WAAQNVVESG GSLQVSHDID
SAYAGADVVY AKSWGALPFF GNWEPEKPIR DQYQHFIVDE RKMALTNNGV FSHCLPLRRN
VKATDAVMDS PNCIAIDEAE NRLHVQKAIM AALASQAGIG NRE
