ID A0A1S6ITB8_9FIRM Unreviewed; 456 AA.
AC A0A1S6ITB8;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-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=B0537_02210 {ECO:0000313|EMBL:AQS58016.1};
OS Desulforamulus ferrireducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC Desulforamulus.
OX NCBI_TaxID=1833852 {ECO:0000313|EMBL:AQS58016.1, ECO:0000313|Proteomes:UP000189464};
RN [1] {ECO:0000313|EMBL:AQS58016.1, ECO:0000313|Proteomes:UP000189464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSS09 {ECO:0000313|EMBL:AQS58016.1,
RC ECO:0000313|Proteomes:UP000189464};
RX PubMed=27153808; DOI=10.1099/ijsem.0.001139;
RA Yang G., Guo J., Zhuang L., Yuan Y., Zhou S.;
RT "Desulfotomaculum ferrireducens sp. nov., a moderately thermophilic
RT sulfate-reducing and dissimilatory Fe(III)-reducing bacterium isolated from
RT compost.";
RL Int. J. Syst. Evol. Microbiol. 66:3022-3028(2016).
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; CP019698; AQS58016.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1S6ITB8; -.
DR STRING; 1833852.B0537_02210; -.
DR KEGG; dfg:B0537_02210; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000189464; Chromosome.
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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW Reference proteome {ECO:0000313|Proteomes:UP000189464}.
FT DOMAIN 6..300
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 363..429
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 456 AA; 51025 MW; 1C080E4557632166 CRC64;
MKLWGGRFQK TTDRLVEDFH SSISFDQRLY RQDIQGSIAH ATMLGKVGVI SQEEAAEIVR
GLQELLEEIE SGQVEFDVAA EDIHMNVEQL LTAKIGAVGK KLHTARSRND QVAVDIRLYL
KDEITVIRQQ LKELIETLLD LAEQHLHTVM PGYTHLQRAQ PITLAHHLMA YTQMFLRDRE
RLADCYKRAD VLPLGSGALA GTTFPLDREY TAELLGFAEV SDNSLDAVSD RDFAVEFCAA
ASLIMMHLSR FCEEIILWSS GEFAFIELDD AYSTGSSIMP QKKNPDVAEL IRGKTGRVYG
DLLGLLTMLK GLPLAYNKDM QEDKEALFDA IDTVKGCLMV FRPMLATMTV RRENMAQAAR
GGFTNATDVA DYLAKKGVPF REAHEIVGKA VFYCLQHNKN LEELTLQEYQ ELSPVFAEDI
YDAIGVEYCA AARKVRGGPA PEAVLQAIAR TRARLE
//
