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Database: UniProt
Entry: A0A2T6B5C3_9RHOB
LinkDB: A0A2T6B5C3_9RHOB
Original site: A0A2T6B5C3_9RHOB 
ID   A0A2T6B5C3_9RHOB        Unreviewed;       507 AA.
AC   A0A2T6B5C3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
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=C8N44_10311 {ECO:0000313|EMBL:PTX51268.1};
OS   Allosediminivita pacifica.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Allosediminivita.
OX   NCBI_TaxID=1267769 {ECO:0000313|EMBL:PTX51268.1, ECO:0000313|Proteomes:UP000244069};
RN   [1] {ECO:0000313|EMBL:PTX51268.1, ECO:0000313|Proteomes:UP000244069}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 29329 {ECO:0000313|EMBL:PTX51268.1,
RC   ECO:0000313|Proteomes:UP000244069};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (APR-2018) 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:PTX51268.1}.
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DR   EMBL; QBKN01000003; PTX51268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T6B5C3; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000244069; 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|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:PTX51268.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244069}.
FT   DOMAIN          107..311
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          376..416
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   507 AA;  55423 MW;  CF047AB64467B97D CRC64;
     MNTDRTMNTN ATDDRTRFPD PVYKDTVLAP LFDHARDDHA EGFRRIDRAH LVMLEKTGIL
     QRDVAGRIAR ALVEIDETVD PAQLEYTGEV EDYFFLREAE LKARVGADTG GRLHTARSRN
     DIDHTLFKMA LKARLAALLD EARALLSAMI DTAEREAETL IVAYTHGQPA QPTTFGHYLG
     AAIEVLIRDI ERLEAAHAVA DLSSMGAAAI TTSGFPVDRA LVAELLGFGA PQRNSYSCIA
     AVDYTTGAYA AVELLFLHLG RLIQDFQVWS SFEVAQIYVP NAFVQISSIM PQKRNPVPIE
     HMRHLSSQAM GKARMMKDIM HNTPFTDMND SEGESQQAGY GAFETGSRVL RLLAAFVPAL
     KINPDRVAAN IDRACITITE LADTLVRHEG LSFRQAHEIA AATAKAVVAE GASLSAGFTP
     FAAAFREATD RETTMDEAGF AEAVSPEYFV AVRDRFGGPA PVAMAEAITA YRAVLSRFED
     TARARHAQET RAAEALDAAF NALTEAC
//
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