ID A0A2P6P616_ROSCH Unreviewed; 1028 AA.
AC A0A2P6P616;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Adenylosuccinate lyase {ECO:0000256|ARBA:ARBA00017058};
DE EC=4.3.2.2 {ECO:0000256|ARBA:ARBA00012339};
DE AltName: Full=Adenylosuccinase {ECO:0000256|ARBA:ARBA00030717};
GN ORFNames=RchiOBHm_Chr7g0194071 {ECO:0000313|EMBL:PRQ17356.1};
OS Rosa chinensis (China rose).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Rosoideae; Rosoideae incertae sedis;
OC Rosa.
OX NCBI_TaxID=74649 {ECO:0000313|EMBL:PRQ17356.1, ECO:0000313|Proteomes:UP000238479};
RN [1] {ECO:0000313|EMBL:PRQ17356.1, ECO:0000313|Proteomes:UP000238479}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Old Blush {ECO:0000313|Proteomes:UP000238479};
RA Bendahmane M.;
RT "The Rosa genome provides new insights in the design of modern roses.";
RL Nat. Genet. 0:0-0(2018).
CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; AMP
CC from IMP: step 2/2. {ECO:0000256|ARBA:ARBA00004734}.
CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-
CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-
CC phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004706}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase
CC subfamily. {ECO:0000256|ARBA:ARBA00008273}.
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:PRQ17356.1}.
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DR EMBL; PDCK01000045; PRQ17356.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6P616; -.
DR STRING; 74649.A0A2P6P616; -.
DR EnsemblPlants; PRQ17356; PRQ17356; RchiOBHm_Chr7g0194071.
DR Gramene; PRQ17356; PRQ17356; RchiOBHm_Chr7g0194071.
DR OMA; AHEVAYP; -.
DR OrthoDB; 203956at2759; -.
DR UniPathway; UPA00074; UER00132.
DR UniPathway; UPA00075; UER00336.
DR Proteomes; UP000238479; Chromosome 7.
DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido) succinate lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd01598; PurB; 2.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 2.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 2.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 2.
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 InterPro; IPR004769; Pur_lyase.
DR InterPro; IPR047136; PurB_bact.
DR InterPro; IPR013539; PurB_C.
DR NCBIfam; TIGR00928; purB; 2.
DR PANTHER; PTHR43411; ADENYLOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43411:SF1; ADENYLOSUCCINATE LYASE; 1.
DR Pfam; PF08328; ASL_C; 2.
DR Pfam; PF00206; Lyase_1; 2.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 2.
DR PROSITE; PS00163; FUMARATE_LYASES; 2.
PE 3: Inferred from homology;
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000313|EMBL:PRQ17356.1};
KW Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000238479}.
FT DOMAIN 131..392
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 409..523
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
FT DOMAIN 604..876
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 892..1006
FT /note="Adenylosuccinate lyase PurB C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08328"
SQ SEQUENCE 1028 AA; 115354 MW; 1646D651E39065F0 CRC64;
MSSKYTTPIL DLNTFRFMNL GLSSRLLHFT PLPPKSQKPT DPSSFNLYLH PPNASLAFPL
RDCALRAAAA KDGNFSGDNE HPDLTALSPL DGRYSGVVKE LAPYLSEYGL IYYRVLVEIK
WLLKLSQIPE VIEVPNFSEE AQSYLQGIID GFSINDAREV KRIEKTTNHD VKAVEYFLKQ
RSSSHPEIAK VLEFYHFACT SEDINNIAHA LMLTESVNNV LLPVMDDLIR AICDMAKEHA
AIPMLSRTHG QTASPTTLGK EMAVFAVRLS TQRQEVSQVA IMGKLAGAVG NYNAHMVAYP
NIDWPLVAEE FVTSLGVSFN PYVTQIETHD YMAKLFHAYI RFNNILIDFD CDIWRYISLG
YFKQTTKAGE IGSSTMPHKV NPIDFENSEG NLGMASGVFS YLSDKLPKSR LQRDLTDSTV
LRNMGVGFGH SLLAYKSTLR GISKLQVNEG RISEDLNHSW EVLAEPIQTV MRRYDVPEPY
EKLKVLTRGR TVTAESIKEF VKGLELPEEP KNILSKLTPH SYVGSAVVLA KTVDVAVRAT
IKDTNVPAEK VKMVFGSSSC ELELSSLLAL SPLDGRYWGK VKDLAPYMSE YGLIYFRVIV
EIKWLLWLSQ IPEVIEVTSF GESAQSFLQE IIDGFSINDA LEIKEIEKVT NHDVKAVEYF
LKQRCKSHPE IAKVLEFFHF ACTSEDINNL AHALMLKGAM NNVMFPIIGD LVQALCTMAK
EYSHIPMLSR THGQPASPTT LGKEMAIFAV RLSREWKEMS CVDIMGKLAG AVGNYNAHEV
AYPDVNWPQV NKEFVRSLGL SFNSYVTQIE PHDYMAELFQ AIFRFNNILT DFDRDVWDYI
SLGYFKQTTK AGEIGSSTMP HKVNPIDFEN SEGNLGVANG NFLHQSMKLP ISRWQRDLTD
STVLRNMGLG LGHSLLAYKS TLQGISKLQV NEACIFEDLN QCWEVLAEPI QTVMRRYGVP
EPYEKLKELT RGKAVTKESI REFTKGLELP DEAKTILLNL TPHSYVGAAI ELARMVDIAV
NSEIGDLS
//
