AOTC_XYLFA
ID AOTC_XYLFA Reviewed; 336 AA.
AC Q9PEN0;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=XF_0998;
OS Xylella fastidiosa (strain 9a5c).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xylella.
OX NCBI_TaxID=160492;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9a5c;
RX PubMed=10910347; DOI=10.1038/35018003;
RA Simpson A.J.G., Reinach F.C., Arruda P., Abreu F.A., Acencio M.,
RA Alvarenga R., Alves L.M.C., Araya J.E., Baia G.S., Baptista C.S.,
RA Barros M.H., Bonaccorsi E.D., Bordin S., Bove J.M., Briones M.R.S.,
RA Bueno M.R.P., Camargo A.A., Camargo L.E.A., Carraro D.M., Carrer H.,
RA Colauto N.B., Colombo C., Costa F.F., Costa M.C.R., Costa-Neto C.M.,
RA Coutinho L.L., Cristofani M., Dias-Neto E., Docena C., El-Dorry H.,
RA Facincani A.P., Ferreira A.J.S., Ferreira V.C.A., Ferro J.A., Fraga J.S.,
RA Franca S.C., Franco M.C., Frohme M., Furlan L.R., Garnier M., Goldman G.H.,
RA Goldman M.H.S., Gomes S.L., Gruber A., Ho P.L., Hoheisel J.D.,
RA Junqueira M.L., Kemper E.L., Kitajima J.P., Krieger J.E., Kuramae E.E.,
RA Laigret F., Lambais M.R., Leite L.C.C., Lemos E.G.M., Lemos M.V.F.,
RA Lopes S.A., Lopes C.R., Machado J.A., Machado M.A., Madeira A.M.B.N.,
RA Madeira H.M.F., Marino C.L., Marques M.V., Martins E.A.L., Martins E.M.F.,
RA Matsukuma A.Y., Menck C.F.M., Miracca E.C., Miyaki C.Y.,
RA Monteiro-Vitorello C.B., Moon D.H., Nagai M.A., Nascimento A.L.T.O.,
RA Netto L.E.S., Nhani A. Jr., Nobrega F.G., Nunes L.R., Oliveira M.A.,
RA de Oliveira M.C., de Oliveira R.C., Palmieri D.A., Paris A., Peixoto B.R.,
RA Pereira G.A.G., Pereira H.A. Jr., Pesquero J.B., Quaggio R.B.,
RA Roberto P.G., Rodrigues V., de Rosa A.J.M., de Rosa V.E. Jr., de Sa R.G.,
RA Santelli R.V., Sawasaki H.E., da Silva A.C.R., da Silva A.M.,
RA da Silva F.R., Silva W.A. Jr., da Silveira J.F., Silvestri M.L.Z.,
RA Siqueira W.J., de Souza A.A., de Souza A.P., Terenzi M.F., Truffi D.,
RA Tsai S.M., Tsuhako M.H., Vallada H., Van Sluys M.A., Verjovski-Almeida S.,
RA Vettore A.L., Zago M.A., Zatz M., Meidanis J., Setubal J.C.;
RT "The genome sequence of the plant pathogen Xylella fastidiosa.";
RL Nature 406:151-159(2000).
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; AE003849; AAF83808.1; -; Genomic_DNA.
DR PIR; F82737; F82737.
DR RefSeq; WP_010893517.1; NC_002488.3.
DR AlphaFoldDB; Q9PEN0; -.
DR SMR; Q9PEN0; -.
DR STRING; 160492.XF_0998; -.
DR EnsemblBacteria; AAF83808; AAF83808; XF_0998.
DR KEGG; xfa:XF_0998; -.
DR eggNOG; COG0078; Bacteria.
DR HOGENOM; CLU_043846_3_3_6; -.
DR OMA; VYVKNWS; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000000812; 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;
KW Reference proteome; Transferase.
FT CHAIN 1..336
FT /note="N-acetylornithine carbamoyltransferase"
FT /id="PRO_0000113269"
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 336 AA; 37623 MW; 5B909F441AA37438 CRC64;
MALKHFLNTQ DWSCSELNAL LTQARAFKHN KLGNGLKGKS IALVFFNASM RTRSSFELGA
FQLGGHAIVL QPGKDAWPIE FDTGTVMEAE TEEHICEVAR VLGHYVDLIG VRAFPKFLDW
TYDRQDIVLN GFAKYSPVPV INMETITHPC QELAHIMALQ EHFGTTDLRG KKYVLTWTYH
PKPLNTAVAN SALTIATRLG MDVTLLCPTP DYVLDERYID WAQQNIADTG STFQVSHDID
NAYRGADVIY AKSWGALPFF GNWAMEKPIR DQYRHFIVDE AKMALTNNAV FSHCLPLRRN
VKATDAVMDG PNCIAIHEAG NRLHVQKAIM AALASQ
