ID A0A063ZHZ4_9EURY Unreviewed; 494 AA.
AC A0A063ZHZ4;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN ORFNames=EL22_05255 {ECO:0000313|EMBL:KDE58373.1};
OS Halostagnicola sp. A56.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Halostagnicola.
OX NCBI_TaxID=1495067 {ECO:0000313|EMBL:KDE58373.1, ECO:0000313|Proteomes:UP000027027};
RN [1] {ECO:0000313|EMBL:KDE58373.1, ECO:0000313|Proteomes:UP000027027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A56 {ECO:0000313|EMBL:KDE58373.1,
RC ECO:0000313|Proteomes:UP000027027};
RA Pore S.D., Kanekar S.P., Arora P., Saxena N., Dhakephalkar P.K.;
RT "Draft genome of Halostagnicola sp. A56 isolated from Andaman Islands,
RT India.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00006};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3. {ECO:0000256|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
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:KDE58373.1}.
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DR EMBL; JMIP02000019; KDE58373.1; -; Genomic_DNA.
DR RefSeq; WP_050051416.1; NZ_JMIP02000019.1.
DR AlphaFoldDB; A0A063ZHZ4; -.
DR STRING; 1495067.EL22_05255; -.
DR OrthoDB; 27337at2157; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000027027; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 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; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:KDE58373.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000027027}.
FT DOMAIN 36..307
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 370..441
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 436..470
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 494 AA; 52604 MW; 2093EF3EC5FFB92A CRC64;
MTGENADGGN ADGNSEGVVR RERFSSGPAR SFLSSLEADA RIFEADLEVD RAHVVMLAER
GIIEPTVAGD ILTALDAIEV EGHENLPDGE DVHEAIETAV IEQVGPDGGK MHTARSRNDE
VATCIRYRLR EDVLSAIETT LALRETLLEV ADEHAETTMP GYTHLQPAQP ITVGHWALSY
ENAVRRDTAR LLDAYGRINQ SPLGGAAFAG TTFDIDRERT ADLLGFDSVL ENSMDASSSR
DFLLETTQTL STHATTLSGL AEDVIIFANR GFVSLSDDYS STSSIMPQKK NPDTLELVRA
VAGDAAGEVQ GLTTTLKGLP RAYNRDLQRA TTHAWEAVDA VRDAAEVTAG AVATADWNEA
ELADEAGAGF STATGVADLL AANGLPFRTA HEVVARAAEA DTDDEFEAVE AAAAEVLGEP
LESYVDPAAV EAALDPAESV ASRDSKGGPA PSTVRDQLES GRQALEADRE EFDDLEDRLA
SAHALLRQEV GAYV
//
