ID   ARLY_ALIF1              Reviewed;         624 AA.
AC   Q5E2E8;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   25-MAY-2022, entry version 109.
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=VF_2303;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW86798.1; -; Genomic_DNA.
DR   RefSeq; WP_011262710.1; NC_006840.2.
DR   RefSeq; YP_205686.1; NC_006840.2.
DR   AlphaFoldDB; Q5E2E8; -.
DR   SMR; Q5E2E8; -.
DR   STRING; 312309.VF_2303; -.
DR   EnsemblBacteria; AAW86798; AAW86798; VF_2303.
DR   KEGG; vfi:VF_2303; -.
DR   PATRIC; fig|312309.11.peg.2341; -.
DR   eggNOG; COG0165; Bacteria.
DR   eggNOG; COG1246; Bacteria.
DR   HOGENOM; CLU_027272_2_3_6; -.
DR   OMA; KKNPDVF; -.
DR   OrthoDB; 751464at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000000537; Chromosome I.
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_0000137846"
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;  69176 MW;  4C66FEE682572EDD CRC64;
     MALWGGRFSQ AADTRFKQFN DSLRIDYRLA EQDIVGSIAW SKALLSVGVI TELEQQKLEL
     ALNELKLEVM EDPEQILLSD AEDIHSWVET QLIGKVGDLG KKLHTGRSRN DQVATDLKLW
     CRQQGHQLLR TLDQLLNQLV NVASEHQATV LPGYTHLQRA QPVTFAHWCL AYVEMIERDY
     SRLEDAINRL DTCPLGSGAL AGTAYPMDRE KLARNLGFQR ATRNSLDSVS DRDHVMELMS
     IASISMLHLS RLAEDMIFYN SGESNFIELA DTVTSGSSLM PQKKNPDALE LIRGKCGRVY
     GAMAGMMMTV KALPLAYNKD MQEDKEGLFD ALDSWSDCIE MAALCFEGIK INGERTLEAA
     KQGYANSTEL ADYLVAKGIP FREAHHIVGV AVVGAIEKGC ALEELSLAEL KAFSEVIEDD
     VYEILTIESC LAKRCALGGV APEQVAYAVE QAGKRLQERD NAGVKVRPAR LTDLDALEGM
     VAYWAGLGEN LPRNRNELVR DIGSFAVAEH HGEVTGCASL YVYDSGLAEI RSLGVEAGWQ
     SQGQGKAIVQ HLVEKAREMA IKKVFVLTRV PEFFMKQDFI PTSRSLLPEK VLKDCDQCPR
     QHACDEVALE VNLQEQVIIK SSVA