ID   ARLY_VIBPA              Reviewed;         624 AA.
AC   P59620;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   23-APR-2003, sequence version 1.
DT   25-MAY-2022, entry version 117.
DE   RecName: Full=Bifunctional protein ArgH;
DE   Includes:
DE     RecName: Full=Argininosuccinate lyase;
DE              Short=ASAL;
DE              EC=4.3.2.1;
DE     AltName: Full=Arginosuccinase;
DE   Includes:
DE     RecName: Full=Probable acetyltransferase;
DE              EC=2.3.1.-;
GN   Name=argH; OrderedLocusNames=VP2756;
OS   Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=223926;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIMD 2210633;
RX   PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA   Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA   Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA   Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT   "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT   distinct from that of V. cholerae.";
RL   Lancet 361:743-749(2003).
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   -!- 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   -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC       Argininosuccinate lyase subfamily. {ECO:0000305}.
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DR   EMBL; BA000031; BAC61019.1; -; Genomic_DNA.
DR   RefSeq; NP_799135.1; NC_004603.1.
DR   RefSeq; WP_005465154.1; NC_004603.1.
DR   AlphaFoldDB; P59620; -.
DR   SMR; P59620; -.
DR   STRING; 223926.28807766; -.
DR   EnsemblBacteria; BAC61019; BAC61019; BAC61019.
DR   GeneID; 1190306; -.
DR   KEGG; vpa:VP2756; -.
DR   PATRIC; fig|223926.6.peg.2652; -.
DR   eggNOG; COG0165; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_027272_2_3_6; -.
DR   OMA; KKNPDVF; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000002493; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008080; F:N-acetyltransferase activity; IEA:InterPro.
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; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR029419; Arg_succ_lyase_C.
DR   InterPro; IPR009049; Argininosuccinate_lyase.
DR   InterPro; IPR011244; ASAL_AGS_AcTrfase.
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; IPR000182; GNAT_dom.
DR   InterPro; IPR008948; L-Aspartase-like.
DR   PANTHER; PTHR43814; PTHR43814; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF14698; ASL_C2; 1.
DR   Pfam; PF00206; Lyase_1; 1.
DR   PIRSF; PIRSF036456; ASAL_AGS; 1.
DR   PRINTS; PR00149; FUMRATELYASE.
DR   SUPFAM; SSF48557; SSF48557; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   TIGRFAMs; TIGR00838; argH; 1.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Lyase; Multifunctional enzyme; Reference proteome; Transferase.
FT   CHAIN           1..624
FT                   /note="Bifunctional protein ArgH"
FT                   /id="PRO_0000137847"
FT   DOMAIN          464..614
FT                   /note="N-acetyltransferase"
FT   REGION          1..466
FT                   /note="Argininosuccinate lyase"
FT   REGION          467..624
FT                   /note="Probable acetyltransferase"
SQ   SEQUENCE   624 AA;  69358 MW;  DA5D4C815438ABCF CRC64;
     MALWGGRFTQ AADTRFKEFN DSLRFDYRLA EQDIVGSIAW SKALLSVGVL SAEEQQKLEL
     ALNELKLEVM EDPHQILRSD AEDIHSWVEQ QLISKVGDLG KKLHTGRSRN DQVATDLKLW
     CRQQGQQLLI ALDRLQSQMV QVAKQHQGTV LPGYTHLQRA QPVTFAHWCL AYVEMFERDY
     SRLSDALQRL DTCPLGSGAL AGTAYPIDRE QLAHNLGFHR ATRNSLDSVS DRDHVMELMS
     VASISMLHLS RLAEDMIFYN SGESNFIELA DTVTSGSSLM PQKKNPDALE LIRGKTGRVY
     GALAGMMMTV KALPLAYNKD MQEDKEGLFD ALDTWNDCME MAALCFDGIK VNGERTLEAA
     KQGYANATEL ADYLVAKGIP FREAHHIVGV AVVGAIAKGC ALEELSLQEL QEFSDVIDND
     VYDILTIESC LEKRSALGGV SPKQVAYAVD QADKRLAQRD SSAVKVRPAR LTDIETLEGM
     VAYWANMGEN LPRSRNELVR DIGSFAVAEH HGEVTGCASL YVYDSGLAEI RSLGIEAGWQ
     GQGQGSAIVN YLVDKARQMA IKKVFVLTRT PEFFMKQSFL PTSKSLLPEK VLKDCDQCPR
     QHACDEVALE INLVEQIIQR SHVA