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Database: UniProt
Entry: A0A0A6CZE3_9SPHN
LinkDB: A0A0A6CZE3_9SPHN
Original site: A0A0A6CZE3_9SPHN 
ID   A0A0A6CZE3_9SPHN        Unreviewed;       442 AA.
AC   A0A0A6CZE3;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE            Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE            EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, 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=NI18_05360 {ECO:0000313|EMBL:KHA64971.1};
OS   Sphingomonas sp. Ant20.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=104605 {ECO:0000313|EMBL:KHA64971.1, ECO:0000313|Proteomes:UP000033201};
RN   [1] {ECO:0000313|EMBL:KHA64971.1, ECO:0000313|Proteomes:UP000033201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Ant20 {ECO:0000313|EMBL:KHA64971.1,
RC   ECO:0000313|Proteomes:UP000033201};
RA   Ronca S., Frossard A., Guerrero L.D., Makhalanyane T.P., Aislabie J.M.,
RA   Cowan D.A.;
RT   "Draft Genome Sequence of Spingomonas sp. strain Ant20, isolated from oil-
RT   polluted soil near Scott Base, Antarctica.";
RL   Submitted (OCT-2014) 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;
CC         Evidence={ECO:0000256|ARBA:ARBA00000985, 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.
CC       {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-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:KHA64971.1}.
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DR   EMBL; JRVI01000024; KHA64971.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6CZE3; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000033201; 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; IPR020557; Fumarate_lyase_CS.
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.
DR   PROSITE; PS00163; FUMARATE_LYASES; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033201}.
FT   DOMAIN          2..285
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          348..417
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   442 AA;  47420 MW;  B25C0CC6570BA255 CRC64;
     MREINASIPF DKRLWKQDIA GSKAHVAMLG AQGIVSPDDA ATIAAGLDRV AAHYAANGVA
     EDLVLEDIHM QTEARLAEAI GPVAGRLHTA RSRNDQVATD FRLWVRDAID QVLAALGGFQ
     AALLVRAEEH AASVMPGFTH LQSAQPVTLG HHLMAYHAMI ARDVSRFADA RVRMNRSPLG
     SAALAGTGFP IDREMTAHAL GFDGPMTNSL DGVSDRDFAL DYLVAATQCA LHLSRLAEEF
     VLWASQPFGF VALSDQWSTG SSIMPQKRNP DAAELVRGHS GRIMGCMTAL MVTMKGLPLA
     YSKDMQDDKP PVFEAHDLLA LSIAAMTGMV ESATFRTERM RAVAEAGFAT ATDLADWLVR
     EAGLPFREAH HVTGRAVKRA EDLGITLDAL SIGDLKAIDA RIDDRVYGVL SVDASVASRT
     SFGGTAPDNV RAAIRAARET SE
//
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