ID A0A558AQE9_9PSEU Unreviewed; 603 AA.
AC A0A558AQE9;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 19.
DE SubName: Full=Ketopantoate reductase {ECO:0000313|EMBL:TVT26501.1};
GN ORFNames=FNH05_31325 {ECO:0000313|EMBL:TVT26501.1};
OS Amycolatopsis rhizosphaerae.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=2053003 {ECO:0000313|EMBL:TVT26501.1, ECO:0000313|Proteomes:UP000320011};
RN [1] {ECO:0000313|EMBL:TVT26501.1, ECO:0000313|Proteomes:UP000320011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBRC 6029 {ECO:0000313|EMBL:TVT26501.1,
RC ECO:0000313|Proteomes:UP000320011};
RA Duangmal K., Teo W.F.A.;
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:TVT26501.1, ECO:0000313|Proteomes:UP000320011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBRC 6029 {ECO:0000313|EMBL:TVT26501.1,
RC ECO:0000313|Proteomes:UP000320011};
RA Srisuk N.;
RT "Amycolatopsis acidicola sp. nov., isolated from peat swamp forest soil.";
RL Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
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:TVT26501.1}.
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DR EMBL; VJWX01000489; TVT26501.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A558AQE9; -.
DR OrthoDB; 9770030at2; -.
DR Proteomes; UP000320011; Unassembled WGS sequence.
DR GO; GO:0004792; F:thiosulfate-cyanide sulfurtransferase activity; IEA:UniProtKB-EC.
DR CDD; cd01448; TST_Repeat_1; 1.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.40.250.10; Rhodanese-like domain; 2.
DR InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR InterPro; IPR013328; 6PGD_dom2.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR001763; Rhodanese-like_dom.
DR InterPro; IPR036873; Rhodanese-like_dom_sf.
DR InterPro; IPR001307; Thiosulphate_STrfase_CS.
DR InterPro; IPR045078; TST/MPST-like.
DR PANTHER; PTHR11364:SF27; SULFURTRANSFERASE; 1.
DR PANTHER; PTHR11364; THIOSULFATE SULFERTANSFERASE; 1.
DR Pfam; PF02558; ApbA; 1.
DR Pfam; PF08546; ApbA_C; 1.
DR Pfam; PF00581; Rhodanese; 2.
DR SMART; SM00450; RHOD; 2.
DR SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 2.
DR PROSITE; PS00380; RHODANESE_1; 1.
DR PROSITE; PS50206; RHODANESE_3; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000320011};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 338..456
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT DOMAIN 483..593
FT /note="Rhodanese"
FT /evidence="ECO:0000259|PROSITE:PS50206"
FT REGION 503..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 583..603
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 63715 MW; C9AF3ADDC6A1B751 CRC64;
MRYIIIGAGA VGSTVAAQLH LAGIRTVLIA RGKHAAAIRD GGLRYLRPSG EQVVAVPVAS
GAAEVDLAAD DVLVLATKTQ NTEEVLQEWA WRPAGEGLAA DLPVVSLQNG LENERAALRR
FRTVFGAAVW QPSTFLEPGE VSAEGAEKPG IFWLGRYPSG EDPRLDAIAE DFRRADFVVQ
VVPDLPRWKA GKLLANLTNA VHALYGRDDR ITGELQAEAR RVFQAAGMTA ADLAAESEVD
ISAVEVAEIP GRARGGSSTW QSLARGAGSV ETDFLNGEIV LLGRLHGVPT PLNEAVQRRL
AIAANHGEAP GSADPAELPR PVPPVLVSAE ELARQLDSEN PPVLLDVRWK LGDPNGHQHY
LEGHLPGAVY VDLHTELAAP PVPAEGRHPL PDLEALQAAA RRWGVREGVS VVAYDAGGNM
AAARAWWLLR WAGLSEVRLL DGGLAAWGDR PLETGHGRTP EPGDVVLRSG NLPVLTIDEA
AAFPDHGLLL DARAGERYRG EQEPIDPRAG HIPGAVSAPT GDNLAPDGRF RSVSELAGRF
AGLGATDRPV AVYCGSGVTA AHEIAALAAA GIEAALYPGS WSQWSNHPDR PVATGPDPVG
PNR
//
