ID F8E3N3_FLESM Unreviewed; 458 AA.
AC F8E3N3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=Flexsi_0629 {ECO:0000313|EMBL:AEI14306.1};
OS Flexistipes sinusarabici (strain ATCC 49648 / DSM 4947 / MAS 10).
OC Bacteria; Deferribacterota; Deferribacteres; Deferribacterales;
OC Flexistipitaceae; Flexistipes.
OX NCBI_TaxID=717231 {ECO:0000313|EMBL:AEI14306.1, ECO:0000313|Proteomes:UP000006621};
RN [1] {ECO:0000313|EMBL:AEI14306.1, ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RX PubMed=22180813; DOI=10.4056/sigs.2235024;
RA Lapidus A., Chertkov O., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Abt B., Spring S., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA Hugenholtz P., Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Genome sequence of the moderately thermophilic halophile Flexistipes
RT sinusarabici strain (MAS10).";
RL Stand. Genomic Sci. 5:86-96(2011).
RN [2] {ECO:0000313|Proteomes:UP000006621}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 4947 / MAS 10 {ECO:0000313|Proteomes:UP000006621};
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Mikhailova N., Chertkov O.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Flexistipes sinusarabici DSM 4947.";
RL Submitted (JUN-2011) 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002858; AEI14306.1; -; Genomic_DNA.
DR RefSeq; WP_013885811.1; NC_015672.1.
DR AlphaFoldDB; F8E3N3; -.
DR STRING; 717231.Flexsi_0629; -.
DR KEGG; fsi:Flexsi_0629; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_0; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000006621; 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|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:AEI14306.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006621}.
FT DOMAIN 8..302
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 365..432
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 458 AA; 52159 MW; E893DF795D42F844 CRC64;
MAEKLWGGRF SLSTHKLAEE FNASINFDRK LYRFDIKGSI AHVEMLAKQR IIVEDEARQI
KDGLEKIEAE IEEGDFEFRD EDEDIHMAIE KRLHELIGPV AGKLHTARSR NDQVATDFRM
YLRERVDEIS ECLRELMQVI VDKSREKIDV VMPGYTHLQT AQPVLFSQYA MAYFQMFKRD
FLRFKDFRER MNECPLGAGA LAGTTFDIDR DYTAERLGFD KPTSNSLDSV SDRDFALEFL
SAASICGMHL SRISEEMVIF SSAEFAFLDL PDDFCTGSSI MPQKKNPDMP ELIRGKTGRL
YGNMISLFTT LKGLPLAYNK DMQEDKEPVF DSVETLISSL RIFTEMFAKM KLNEKKMAKA
AGGGFSTATD LADYLVRKGM PFREAHNVVG KTVAYALSKN KGLEDLEMEE FRQFSRVIEG
DIFEYVVVAK SVDSRKAKGG TAKSSVLQQI KEAEEFLT
//
