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Database: UniProt
Entry: A0A166K6X7_9HOMO
LinkDB: A0A166K6X7_9HOMO
Original site: A0A166K6X7_9HOMO 
ID   A0A166K6X7_9HOMO        Unreviewed;       547 AA.
AC   A0A166K6X7;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   28-MAR-2018, entry version 9.
DE   SubName: Full=Delta-1-pyrroline-5-carboxylate dehydrogenase {ECO:0000313|EMBL:KZP21596.1};
GN   ORFNames=FIBSPDRAFT_860541 {ECO:0000313|EMBL:KZP21596.1};
OS   Fibularhizoctonia sp. CBS 109695.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina;
OC   Agaricomycetes; Agaricomycetidae; Atheliales; Atheliaceae;
OC   Fibularhizoctonia.
OX   NCBI_TaxID=436010 {ECO:0000313|EMBL:KZP21596.1, ECO:0000313|Proteomes:UP000076532};
RN   [1] {ECO:0000313|EMBL:KZP21596.1, ECO:0000313|Proteomes:UP000076532}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 109695 {ECO:0000313|EMBL:KZP21596.1,
RC   ECO:0000313|Proteomes:UP000076532};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K.,
RA   Labutti K., Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T.,
RA   Yoshinaga Y., Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi
RT   Provides Insights into the Origins of Lignocellulose Decay
RT   Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU003345}.
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DR   EMBL; KV417546; KZP21596.1; -; Genomic_DNA.
DR   EnsemblFungi; KZP21596; KZP21596; FIBSPDRAFT_860541.
DR   Proteomes; UP000076532; Unassembled WGS sequence.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:EnsemblFungi.
DR   GO; GO:0003842; F:1-pyrroline-5-carboxylate dehydrogenase activity; IEA:EnsemblFungi.
DR   GO; GO:0016620; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006537; P:glutamate biosynthetic process; IEA:EnsemblFungi.
DR   GO; GO:0010133; P:proline catabolic process to glutamate; IEA:EnsemblFungi.
DR   CDD; cd07123; ALDH_F4-17_P5CDH; 1.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 2.
DR   InterPro; IPR016161; Ald_DH/histidinol_DH.
DR   InterPro; IPR016163; Ald_DH_C.
DR   InterPro; IPR016160; Ald_DH_CS_CYS.
DR   InterPro; IPR029510; Ald_DH_CS_GLU.
DR   InterPro; IPR016162; Ald_DH_N.
DR   InterPro; IPR015590; Aldehyde_DH_dom.
DR   InterPro; IPR005931; P5CDH/ALDH4A1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; SSF53720; 1.
DR   TIGRFAMs; TIGR01236; D1pyr5carbox1; 1.
DR   PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR   PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000076532};
KW   Oxidoreductase {ECO:0000256|RuleBase:RU003345};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076532}.
FT   DOMAIN       67    518       Aldedh. {ECO:0000259|Pfam:PF00171}.
SQ   SEQUENCE   547 AA;  59329 MW;  40DDF43FBC2661F6 CRC64;
     MANPQLASFK VPAIENEPMR TYALGSAERK GLEAAIAQME KDLPFEVPCI VNGKPVKTGK
     LAKQPMPADH ANHLCSYHEA DQATVAAAID GALAAKAEWE SMPWNDRAAI FLKAADLVSG
     KYRYRLMAAT ILGQGKNAWQ AEIDAAAEFA DFLRFGVKFV EELYSIQPSK NSAGAWNRVE
     YRALEGFVLA VSPFNFTAIG GNLPGAPALL GNVVVWKPSP MATYSNYIIH QIFTEAGVPP
     GVIQFVPGPP AEVVGQAIAH RSFAALHFTG STHVFKQLWK DIANNLDVYK GYPRIVGETG
     GKNFHVVHES ADIKNAVIQT VRGAYEYQGQ KCSALSRLYV SASAWKNGFK DQLLEEIAKI
     KVGAPQDWSN FMGPVINRQS YDKITGYIQK AKDAGGEVLI GGTGDDSKGY FVQPTVILTK
     DPKSVTMVEE IFGPVITAYV FEDADFEKTL ELVDTTTDYS LTGAIFSTSR AALINATNKL
     RNAAGNVYYN EKCTGAVVGQ QPFGGARGSG TNDKAGSISI FYRFVSARSI KENFVGLEEF
     AYPSNLV
//
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