(data stored in ACNUC7421 zone)

SWISSPROT: C6WGG9_ACTMD

ID   C6WGG9_ACTMD            Unreviewed;       125 AA.
AC   C6WGG9;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   07-JUN-2017, entry version 45.
DE   RecName: Full=7,8-dihydroneopterin aldolase {ECO:0000256|RuleBase:RU362079};
DE            EC=4.1.2.25 {ECO:0000256|RuleBase:RU362079};
GN   OrderedLocusNames=Amir_0316 {ECO:0000313|EMBL:ACU34285.1};
OS   Actinosynnema mirum (strain ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU
OS   3971).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Actinosynnema.
OX   NCBI_TaxID=446462 {ECO:0000313|EMBL:ACU34285.1, ECO:0000313|Proteomes:UP000002213};
RN   [1] {ECO:0000313|EMBL:ACU34285.1, ECO:0000313|Proteomes:UP000002213}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29888 / DSM 43827 / NBRC 14064 / IMRU 3971
RC   {ECO:0000313|Proteomes:UP000002213};
RX   PubMed=21304636; DOI=10.4056/sigs.21137;
RA   Land M., Lapidus A., Mayilraj S., Chen F., Copeland A., Del Rio T.G.,
RA   Nolan M., Lucas S., Tice H., Cheng J.F., Chertkov O., Bruce D.,
RA   Goodwin L., Pitluck S., Rohde M., Goker M., Pati A., Ivanova N.,
RA   Mavromatis K., Chen A., Palaniappan K., Hauser L., Chang Y.J.,
RA   Jeffries C.C., Brettin T., Detter J.C., Han C., Chain P.,
RA   Tindall B.J., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Actinosynnema mirum type strain (101).";
RL   Stand. Genomic Sci. 1:46-53(2009).
CC   -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin to 6-
CC       hydroxymethyl-7,8-dihydropterin. {ECO:0000256|RuleBase:RU362079}.
CC   -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8-
CC       dihydropterin + glycolaldehyde. {ECO:0000256|RuleBase:RU362079}.
CC   -!- PATHWAY: Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-
CC       amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate
CC       from 7,8-dihydroneopterin triphosphate: step 3/4.
CC       {ECO:0000256|RuleBase:RU362079}.
CC   -!- SIMILARITY: Belongs to the DHNA family.
CC       {ECO:0000256|RuleBase:RU362079}.
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DR   EMBL; CP001630; ACU34285.1; -; Genomic_DNA.
DR   RefSeq; WP_012782948.1; NC_013093.1.
DR   STRING; 446462.Amir_0316; -.
DR   EnsemblBacteria; ACU34285; ACU34285; Amir_0316.
DR   KEGG; ami:Amir_0316; -.
DR   eggNOG; ENOG4105KRF; Bacteria.
DR   eggNOG; COG1539; LUCA.
DR   HOGENOM; HOG000217628; -.
DR   KO; K01633; -.
DR   OMA; FYAYHGV; -.
DR   OrthoDB; POG091H02IN; -.
DR   UniPathway; UPA00077; UER00154.
DR   Proteomes; UP000002213; Chromosome.
DR   GO; GO:0102083; F:7,8-dihydromonapterin aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046656; P:folic acid biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046654; P:tetrahydrofolate biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd00534; DHNA_DHNTPE; 1.
DR   InterPro; IPR006156; Dihydroneopterin_aldolase.
DR   InterPro; IPR006157; FolB_dom.
DR   Pfam; PF02152; FolB; 1.
DR   SMART; SM00905; FolB; 1.
DR   TIGRFAMs; TIGR00525; folB; 1.
DR   TIGRFAMs; TIGR00526; folB_dom; 1.
PE   3: Inferred from homology;
DR   PRODOM; C6WGG9.
DR   SWISS-2DPAGE; C6WGG9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002213};
KW   Folate biosynthesis {ECO:0000256|RuleBase:RU362079};
KW   Lyase {ECO:0000256|RuleBase:RU362079};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002213}.
FT   DOMAIN       11    123       FolB. {ECO:0000259|SMART:SM00905}.
SQ   SEQUENCE   125 AA;  13582 MW;  2051085473DAFA42 CRC64;
     MAEATGSGDR IELRGLTVRA HHGVFEHEKR DGQDFLVDVV VWLDLTRAAA TDDLRETLHY
     GELAERVAEV VAGGPHDLIE TVAGRAADVV MADGRVTATE VTVHKPHAPI PLIFADVAVT
     VRRTR
//

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