UniProt: A0A0T2KS22

Database: UniProt
Entry: A0A0T2KS22_9MICO

LinkDB:  A0A0T2KS22_9MICO 
Original site:  A0A0T2KS22_9MICO

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (10)   
   InterPro (7)   
   Pfam (2)   
   PROSITE (1)   
All databases (16)   

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ID   A0A0T2KS22_9MICO        Unreviewed;       476 AA.
AC   A0A0T2KS22;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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=ASD65_18620 {ECO:0000313|EMBL:KRA22482.1};
OS   Microbacterium sp. Root61.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=1736570 {ECO:0000313|EMBL:KRA22482.1, ECO:0000313|Proteomes:UP000051216};
RN   [1] {ECO:0000313|EMBL:KRA22482.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA22482.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRA22482.1, ECO:0000313|Proteomes:UP000051216}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root61 {ECO:0000313|EMBL:KRA22482.1,
RC   ECO:0000313|Proteomes:UP000051216};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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;
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:KRA22482.1}.
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DR   EMBL; LMGU01000002; KRA22482.1; -; Genomic_DNA.
DR   RefSeq; WP_056226315.1; NZ_LMGU01000002.1.
DR   AlphaFoldDB; A0A0T2KS22; -.
DR   STRING; 1736570.ASD65_18620; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000051216; 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|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   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|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:KRA22482.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051216}.
FT   DOMAIN          31..312
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          375..443
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   476 AA;  50767 MW;  E0AA36BF53CD68A0 CRC64;
     MSDTKNDGTN EGALWGARFA SGPSPELVAL SRSTHFDWAL ALYDIAGSHA HAKALAAAGY
     LTPDEETRMH AGLDTLAARI TDGSLQPSPS DEDVHGALEQ ALIATVGPEL GGKLRAGRSR
     NDQIATLVRM YLLDHSRTIA RDILRLIDAI VAQAEAHALA IMPGRTHLQH AQPVLLAHHL
     QAHAWPLVRD LERLRDWSAR ASVSPYGGGA LAGSTLGLDP QLVARELGLA RPSENSIDGT
     AARDVVAEFA FIAAQVGIDL SRFAEEIILW NTREFGFVTL HDGYSTGSSI MPQKKNPDIA
     ELARGKSGRL IGNLAGLLAT LKGLPLAYNR DLQEDKEPVF DSIATLEVLL PAFTGMVATL
     RFDTERMAEL APQGFSLATD VAEWLVKTGV PFRDAHEASG RLVQLCEESG IELSEVTDEM
     LAAASPNLSP DVREVLTIEG SVASRAGVGG TAPVRVAEQR AELVARSQTV AHALGL
//

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