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Database: UniProt
Entry: A0A1R4GJJ4_9MICO
LinkDB: A0A1R4GJJ4_9MICO
Original site: A0A1R4GJJ4_9MICO 
ID   A0A1R4GJJ4_9MICO        Unreviewed;       475 AA.
AC   A0A1R4GJJ4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
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=CZ674_12495 {ECO:0000313|EMBL:SJM68284.1};
OS   Agrococcus casei LMG 22410.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Agrococcus.
OX   NCBI_TaxID=1255656 {ECO:0000313|EMBL:SJM68284.1, ECO:0000313|Proteomes:UP000195787};
RN   [1] {ECO:0000313|EMBL:SJM68284.1, ECO:0000313|Proteomes:UP000195787}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 22410 {ECO:0000313|EMBL:SJM68284.1,
RC   ECO:0000313|Proteomes:UP000195787};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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}.
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DR   EMBL; FUHU01000045; SJM68284.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1R4GJJ4; -.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000195787; 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:SJM68284.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000195787}.
FT   DOMAIN          30..315
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          378..445
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"
SQ   SEQUENCE   475 AA;  51525 MW;  05F520ECEBFC0468 CRC64;
     MTEGDAAQRH GTNEGSLWGA RFASGPAPEM AILSKSTHFD WRLAQYDIAG SRAHAIALHA
     ANYLSDDELR GMHSALDELS ARVADGRFQA AESDEDVHGA LERGLIEIAG AELGGRLRAG
     RSRNDQIATL IRLWMRDESE HIVRGLHGMI AALIEQAKAH PNAPMPGRTH LQHAQPVLLS
     HDLLAHAWPL VRDLERLRDW RVRASESPYG GGALAGSSLG LDPRLVAGEL GLGAPSHNSI
     DATSARDVTA EFAYVLTQIG IDLSRLAEEV IFWVTREAGI AKLHDAFSTG SSIMPQKKNP
     DIPELTRGKA GRLIGNLTGL LATLKALPLA YNRDLQEDKE PVFDSVDQLR MVLPAMAGMV
     ATLEFDTDRM RDLAPQGFSL ATDVAEWLVR QGVPFRDAHE VSGELVQFCE ERGLELHEPS
     DDDYRSISEH LLPAVRDVLS VDGAIASRRG VGGTAPDAVA EQLRALEERL ASLVG
//
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