ID A0A2P6TYE4_CHLSO Unreviewed; 708 AA.
AC A0A2P6TYE4;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 13-SEP-2023, entry version 18.
DE SubName: Full=Histidine biosynthesis bifunctional chloroplastic {ECO:0000313|EMBL:PRW59060.1};
GN ORFNames=C2E21_2186 {ECO:0000313|EMBL:PRW59060.1};
OS Chlorella sorokiniana (Freshwater green alga).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Chlorella clade; Chlorella.
OX NCBI_TaxID=3076 {ECO:0000313|EMBL:PRW59060.1, ECO:0000313|Proteomes:UP000239899};
RN [1] {ECO:0000313|EMBL:PRW59060.1, ECO:0000313|Proteomes:UP000239899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UTEX 1602 {ECO:0000313|Proteomes:UP000239899};
RX PubMed=29178410; DOI=10.1111/tpj.13789;
RA Arriola M.B., Velmurugan N., Zhang Y., Plunkett M.H., Hondzo H.,
RA Barney B.M.;
RT "Genome sequences of Chlorella sorokiniana UTEX 1602 and Micractinium
RT conductrix SAG 241.80: implications to maltose excretion by a green alga.";
RL Plant J. 93:566-586(2018).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-
CC D-ribosyl)-5-[(5-phospho-beta-D-
CC ribosylamino)methylideneamino]imidazole-4-carboxamide;
CC Xref=Rhea:RHEA:20049, ChEBI:CHEBI:15377, ChEBI:CHEBI:58435,
CC ChEBI:CHEBI:59457; EC=3.5.4.19;
CC Evidence={ECO:0000256|ARBA:ARBA00000024};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-
CC ribosyl)-5'-AMP + diphosphate + H(+); Xref=Rhea:RHEA:22828,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:59457, ChEBI:CHEBI:73183; EC=3.6.1.31;
CC Evidence={ECO:0000256|ARBA:ARBA00001460};
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9.
CC {ECO:0000256|ARBA:ARBA00005204}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine
CC from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9.
CC {ECO:0000256|ARBA:ARBA00005169}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the PRA-PH family.
CC {ECO:0000256|ARBA:ARBA00007731}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the PRA-CH family.
CC {ECO:0000256|ARBA:ARBA00008299}.
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:PRW59060.1}.
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DR EMBL; LHPG02000004; PRW59060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P6TYE4; -.
DR STRING; 3076.A0A2P6TYE4; -.
DR OrthoDB; 1114at2759; -.
DR UniPathway; UPA00031; UER00007.
DR Proteomes; UP000239899; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11534; NTP-PPase_HisIE_like; 1.
DR Gene3D; 1.10.287.1080; MazG-like; 1.
DR Gene3D; 3.10.20.810; Phosphoribosyl-AMP cyclohydrolase; 1.
DR Gene3D; 4.10.60.10; Zinc finger, CCHC-type; 3.
DR HAMAP; MF_01019; HisIE; 1.
DR InterPro; IPR023019; His_synth_HisIE.
DR InterPro; IPR008179; HisE.
DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like.
DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom.
DR InterPro; IPR038019; PRib_AMP_CycHydrolase_sf.
DR InterPro; IPR001878; Znf_CCHC.
DR InterPro; IPR036875; Znf_CCHC_sf.
DR NCBIfam; TIGR03188; histidine_hisI; 1.
DR PANTHER; PTHR42945; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN; 1.
DR PANTHER; PTHR42945:SF1; HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN HIS7; 1.
DR Pfam; PF01502; PRA-CH; 1.
DR Pfam; PF01503; PRA-PH; 1.
DR Pfam; PF00098; zf-CCHC; 3.
DR SMART; SM00343; ZnF_C2HC; 5.
DR SUPFAM; SSF101386; all-alpha NTP pyrophosphatases; 1.
DR SUPFAM; SSF141734; HisI-like; 1.
DR SUPFAM; SSF57756; Retrovirus zinc finger-like domains; 3.
DR PROSITE; PS50158; ZF_CCHC; 4.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Histidine biosynthesis {ECO:0000256|ARBA:ARBA00023102};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000239899};
KW Zinc {ECO:0000256|PROSITE-ProRule:PRU00047};
KW Zinc-finger {ECO:0000256|PROSITE-ProRule:PRU00047}.
FT DOMAIN 150..164
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 173..188
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 191..205
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT DOMAIN 282..295
FT /note="CCHC-type"
FT /evidence="ECO:0000259|PROSITE:PS50158"
FT REGION 1..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 308..328
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 708 AA; 75434 MW; 7C68CD971984E8CD CRC64;
MEAAVRRRAA ANAAAAADAS QPPKAPPPKS SSPESGELPG SASADGQRQV RQRPARRSSP
AVAPKAAAPA DLDLDLDAEP ASDSSSGGGS SSGSDSEEEA GAERTEPAVP APAPAGVIVV
ETAEQRNAEV QRLLRAPRYF DEDFEEAGLR CFKCGGKGHF ARDCTAEARE RSCFLCAQYG
HDSRDCPNSL CWRCQRPGHM ARDCPYGYRA QPSWDEAGPA VCLRCGSETC PCAGEKDFVR
AEGGCKREYR ERDLRHVRCY SCGKRGHLSC APAPEEPAAL SCHNCGQGGH TAAECNRELP
QVIRGEMAGS SHRASFDRGG GGGGGGYSSG GYGSGGGYRQ QQSGGYGSRQ PRYAAYSAYA
EIEQPHRRRS YDDAFDRDGY GYGRQRAACW PPGAAGLHHW AAALACSARP LLQPRKPQQL
QCCSSARSVR RMRTSSAVAA AATSPAAAAA AAAAAAAPRP VRPEAEVPGM TEFLDRLKWD
ANGLVVAIAQ HADTGEVLMQ AFADRAAVCE TLQTGLATFY SRSRKGRWCK GETSGHFIQV
LSTYMDCDRD SLIYLSDPIG PACHTNAPTC YFTQLDAGSG EMRTAGDHHS QAHVPMTTLF
ALERTIEQRR AEAEAGTSAG GKPSWTAKLL ADPQLLCKKV REEAGELCQT LEADEGKERA
ASEAADLFYH ALVLLNKQGV SLEDVSKVLR SRFGTSGIEE KAARPPKQ
//
