ID A0A0A0EYP9_9GAMM Unreviewed; 338 AA.
AC A0A0A0EYP9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=N-acetylornithine carbamoyltransferase {ECO:0000256|HAMAP-Rule:MF_02234};
DE EC=2.1.3.9 {ECO:0000256|HAMAP-Rule:MF_02234};
DE AltName: Full=N-acetyl-L-ornithine transcarbamylase {ECO:0000256|HAMAP-Rule:MF_02234};
DE Short=AOTCase {ECO:0000256|HAMAP-Rule:MF_02234};
DE Short=Acetylornithine transcarbamylase {ECO:0000256|HAMAP-Rule:MF_02234};
GN Name=argF' {ECO:0000256|HAMAP-Rule:MF_02234};
GN ORFNames=N799_07190 {ECO:0000313|EMBL:KGM55360.1};
OS Lysobacter arseniciresistens ZS79.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=913325 {ECO:0000313|EMBL:KGM55360.1, ECO:0000313|Proteomes:UP000029989};
RN [1] {ECO:0000313|EMBL:KGM55360.1, ECO:0000313|Proteomes:UP000029989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZS79 {ECO:0000313|EMBL:KGM55360.1,
RC ECO:0000313|Proteomes:UP000029989};
RX PubMed=26516404; DOI=10.1186/s40793-015-0070-5;
RA Liu L., Zhang S., Luo M., Wang G.;
RT "Genomic information of the arsenic-resistant bacterium Lysobacter
RT arseniciresistens type strain ZS79(T) and comparison of Lysobacter draft
RT genomes.";
RL Stand. Genomic Sci. 10:88-88(2015).
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. {ECO:0000256|HAMAP-Rule:MF_02234}.
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:0000256|HAMAP-Rule:MF_02234};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC superfamily. AOTCase family. {ECO:0000256|HAMAP-Rule:MF_02234}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KGM55360.1}.
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DR EMBL; AVPT01000019; KGM55360.1; -; Genomic_DNA.
DR RefSeq; WP_036211719.1; NZ_AVPT01000019.1.
DR AlphaFoldDB; A0A0A0EYP9; -.
DR STRING; 913325.N799_07190; -.
DR eggNOG; COG0078; Bacteria.
DR OrthoDB; 9802587at2; -.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000029989; Unassembled WGS sequence.
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; Aspartate/ornithine carbamoyltransferase; 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 PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR45753:SF3; ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL; 1.
DR Pfam; PF00185; OTCace; 1.
DR Pfam; PF02729; OTCace_N; 1.
DR PRINTS; PR00100; AOTCASE.
DR PRINTS; PR00101; ATCASE.
DR SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_02234};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_02234};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_02234};
KW Reference proteome {ECO:0000313|Proteomes:UP000029989};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02234}.
FT DOMAIN 6..163
FT /note="Aspartate/ornithine carbamoyltransferase carbamoyl-P
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02729"
FT DOMAIN 188..334
FT /note="Aspartate/ornithine carbamoyltransferase Asp/Orn-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF00185"
FT BINDING 51..54
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:0000256|HAMAP-Rule:MF_02234"
FT BINDING 79
FT /ligand="carbamoyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58228"
FT /ligand_note="ligand shared between two neighboring
FT subunits"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 114
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:0000256|HAMAP-Rule:MF_02234"
FT BINDING 146
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 150..153
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:0000256|HAMAP-Rule:MF_02234"
FT BINDING 254
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 296..297
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:0000256|HAMAP-Rule:MF_02234"
FT BINDING 297
FT /ligand="N(2)-acetyl-L-ornithine"
FT /ligand_id="ChEBI:CHEBI:57805"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT BINDING 324
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:0000256|HAMAP-Rule:MF_02234"
FT SITE 94
FT /note="Key residue in conferring substrate specificity for
FT N-acetyl-L-ornithine versus N-succinyl-L-ornithine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
FT MOD_RES 304
FT /note="N6-carboxylysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02234"
SQ SEQUENCE 338 AA; 37717 MW; 671324C6A50830F6 CRC64;
MTSTPRHFLN TQDWSRADLD ALLARAAGFK RDRLGDQLRG KSIALVFFNP SMRTRTSFEL
GAFQLGGHAV VLQPGKDAWP IEFDHGTVMD GEAEEHVAEV ARVLGRYADL IGVRAFPKFV
DWSVDREDRV LKAFAKYSPV PVINMETITH PCQELAHAMA LQEHFGTSDL RGRKFVLTWT
YHPKPLNTAV ANSALTIATR MGMDVTLLCP TPEYVLDERY MGWAEANVAE SGGSLAVSHD
IDSAYAGADV VYAKSWGALP YFGNWAPEKP IRDRYKHFIV DERKMALTND GVFSHCLPLR
RNVKATDAVM DSPRCIAIDE AENRLHVQKA VMATLANR
//
