ID   ARGHA_MORPR             Reviewed;         470 AA.
AC   Q9K3D7;
DT   12-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Bifunctional protein ArgHA;
DE   Includes:
DE     RecName: Full=Argininosuccinate lyase;
DE              Short=ASAL;
DE              Short=Arginosuccinase;
DE              EC=4.3.2.1;
DE   Includes:
DE     RecName: Full=Amino-acid acetyltransferase;
DE              EC=2.3.1.1;
DE     AltName: Full=N-acetylglutamate synthase;
DE              Short=AGS;
DE              Short=NAGS;
DE   Flags: Fragment;
GN   Name=argHA;
OS   Moritella profunda.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Moritellaceae; Moritella.
OX   NCBI_TaxID=111291;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=2674;
RX   PubMed=10692366; DOI=10.1128/jb.182.6.1609-1615.2000;
RA   Xu Y., Liang Z., Legrain C., Ruger H.J., Glansdorff N.;
RT   "Evolution of arginine biosynthesis in the bacterial domain: novel gene-
RT   enzyme relationships from psychrophilic Moritella strains (Vibrionaceae)
RT   and evolutionary significance of N-alpha-acetyl ornithinase.";
RL   J. Bacteriol. 182:1609-1615(2000).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC         Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC         ChEBI:CHEBI:57472; EC=4.3.2.1;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-glutamate = CoA + H(+) + N-acetyl-L-glutamate;
CC         Xref=Rhea:RHEA:24292, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:44337, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.1;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-
CC       L-ornithine from L-glutamate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 3/3.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- MISCELLANEOUS: In bacteria which possess the bifunctional enzyme
CC       ornithine acetyltransferase/N-acetylglutamate synthase (ArgJ), ArgA
CC       fulfills an anaplerotic role.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC       Argininosuccinate lyase subfamily. {ECO:0000305}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the acetyltransferase
CC       family. ArgA subfamily. {ECO:0000305}.
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DR   EMBL; AJ252020; CAB95018.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9K3D7; -.
DR   SMR; Q9K3D7; -.
DR   UniPathway; UPA00068; UER00106.
DR   UniPathway; UPA00068; UER00114.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0103045; F:methione N-acyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR   CDD; cd01359; Argininosuccinate_lyase; 1.
DR   Gene3D; 1.10.275.10; -; 1.
DR   HAMAP; MF_00006; Arg_succ_lyase; 1.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR024083; Fumarase/histidase_N.
DR   InterPro; IPR020557; Fumarate_lyase_CS.
DR   InterPro; IPR000362; Fumarate_lyase_fam.
DR   InterPro; IPR022761; Fumarate_lyase_N.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR43814; PTHR43814; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Lyase; Multifunctional enzyme; Transferase.
FT   CHAIN           1..>470
FT                   /note="Bifunctional protein ArgHA"
FT                   /id="PRO_0000186814"
FT   REGION          1..>470
FT                   /note="Argininosuccinate lyase"
FT   NON_TER         470
SQ   SEQUENCE   470 AA;  51907 MW;  68046071CE1F761E CRC64;
     MALWGGRFSQ AADARFKNFN DSLRFDYRLA EQDITGSVAW SKALVSVGIL TQDEQLTIEA
     ALNDLKLAVL ENPEQILQSD AEDIHSWVET QLIAKVGDLG KKLHTGRSRN DQVATDLKLW
     CKQQGEQLLM QLDKTQQQLV SLAREHQHTV LPGYTHLQRA QPVTFSHWCL AYVEMLERDF
     SRLTDCLKRL DTCPLGSGAL AGTAYPMDRT ELAHTLGFAS ATLNSLDSVS DRDHVMELMS
     TASMSMIHLS RLAEDLIFYN SGESNFIELA DAVTSGSSLM PQKKNPDALE LIRGKTGRVF
     GSLSAMLMTL KALPLAYNKD MQEDKEGLFD ALDTWSDCLE MAAMSLVGMK INEERTKEAA
     LGGYSNATEL ADYLVAKGVP FRDSHHIVGE AVVAAIAKGV PLEALTLAEF KAFDVLIEDD
     VYHHLSLDET LAKRKAQGGV SPVQVEFALT NAEKRLEERD TSGISIRAAR