Reviewed, UniProtKB/Swiss-Prot Q31IR4 (PDXH1_THICR)

Names and origin

Protein names

Recommended name:
    Pyridoxine/pyridoxamine 5'-phosphate oxidase 1
    EC=1.4.3.5
Alternative name(s):
    PNP/PMP oxidase 1
      Short name=PNPOx 1
    Pyridoxal 5'-phosphate synthase 1

Gene names

Name:	pdxH1
Ordered Locus Names:	Tcr_0363

Organism

Thiomicrospira crunogena (strain XCL-2) [Complete proteome] [HAMAP]

Taxonomic identifier

317025 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Thiotrichales › Piscirickettsiaceae › Thiomicrospira

Protein attributes

Sequence length	216 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Catalyzes the oxidation of either pyridoxine 5'-phosphate (PNP) or pyridoxamine 5'-phosphate (PMP) into pyridoxal 5'-phosphate (PLP) By similarity.
Catalytic activity	Pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2. HAMAP MF_01629 Pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2. HAMAP MF_01629
Cofactor	Binds 1 FMN per subunit By similarity.
Pathway	Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxamine 5'-phosphate: step 1/1. HAMAP MF_01629 Cofactor biosynthesis; B6 vitamer interconversion; pyridoxal 5'-phosphate from pyridoxine 5'-phosphate: step 1/1.
Subunit structure	Homodimer By similarity.
Sequence similarities	Belongs to the pyridoxamine 5'-phosphate oxidase family.

Ontologies

Keywords
Biological process	Pyridoxine biosynthesis
Ligand	FMN Flavoprotein
Molecular function	Oxidoreductase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW pyridoxine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FMN binding Inferred from electronic annotation. Source: HAMAP pyridoxamine-phosphate oxidase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 216	216	Pyridoxine/pyridoxamine 5'-phosphate oxidase 1 HAMAP MF_01629		PRO_0000255894
Regions
	Nucleotide binding	78 – 79	2	FMN By similarity
	Nucleotide binding	142 – 143	2	FMN By similarity
	Region	10 – 13	4	Substrate binding By similarity
	Region	192 – 194	3	Substrate binding By similarity
Sites
	Binding site	63	1	FMN By similarity
	Binding site	66	1	FMN; via amide nitrogen By similarity
	Binding site	68	1	Substrate By similarity
	Binding site	85	1	FMN By similarity
	Binding site	125	1	Substrate By similarity
	Binding site	129	1	Substrate By similarity
	Binding site	133	1	Substrate By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q31IR4-1 [UniParc]. Last modified December 6, 2005. Version 1. Checksum: 31FFE39B0E9EFD58	FASTA	216	25,160
	10 20 30 40 50 60 MPNRDYHAER REYGFAALRR ADLQTDPFHQ FSDWMETALE KTQQDATAMS VSTVSADGQP 70 80 90 100 110 120 HSRIVLLKTF NSDGFIFYTH YDSDKGQQID QNAKAALLFF WPELDRQIRI EGSLQKVPRE 130 140 150 160 170 180 TSEAYFHSRP KDSQLAASIS NQSQPVASRD ILEAKLQEAM SLPDRNLTCP AHWGGYQLKP 190 200 210 CYFEFWQGRP SRLHDRFRYQ RLSKNDQAWQ ITRLNP

References

[1]

"The genome of deep-sea vent chemolithoautotroph Thiomicrospira crunogena XCL-2." Scott K.M., Sievert S.M., Abril F.N., Ball L.A., Barrett C.J., Blake R.A., Boller A.J., Chain P.S.G., Clark J.A., Davis C.R., Detter C., Do K.F., Dobrinski K.P., Faza B.I., Fitzpatrick K.A., Freyermuth S.K., Harmer T.L., Hauser L.J. , Huegler M., Kerfeld C.A., Klotz M.G., Kong W.W., Land M., Lapidus A., Larimer F.W., Longo D.L., Lucas S., Malfatti S.A., Massey S.E., Martin D.D., McCuddin Z., Meyer F., Moore J.L., Ocampo L.H. Jr., Paul J.H., Paulsen I.T., Reep D.K., Ren Q., Ross R.L., Sato P.Y., Thomas P., Tinkham L.E., Zeruth G.T. PLoS Biol. 4:1-17(2006) [PubMed: 17105352] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBLGenBankDDBJ	CP000109 Genomic DNA. Translation: ABB40959.1.
RefSeq	YP_390633.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
STRING	Q31IR4.
Genome annotation databases
GeneID	3762349.
GenomeReviews	Gene locus Tcr_0363 in contig CP000109_GR.
KEGG	tcx:Tcr_0363.
NMPDR	fig|317025.3.peg.332.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	Q31IR4.
OMA	RKGSELE.
Enzyme and pathway databases
BioCyc	TCRU317025:TCR_0363-MON.
Family and domain databases
HAMAP	MF_01629. [Tree]
InterPro	IPR000659. Pyridoxamine_oxidase. IPR019740. Pyridoxamine_oxidase_CS. IPR019576. Pyridoxamine_oxidase_dimer_C. IPR011576. PyridoxamineP_oxidase_FMN-bd. IPR012349. Split_barrel_FMN_bd. [Graphical view]
Gene3D	G3DSA:2.30.110.10. PNPOx_FMN_bd. 1 hit.
PANTHER	PTHR10851. Pyridox_oxidase. 1 hit.
Pfam	PF10590. PNPOx_C. 1 hit. PF01243. Pyridox_oxidase. 1 hit. [Graphical view]
ProDom	PD006312. Pyridox_oxidase. 1 hit. [Graphical view] [Entries sharing at least one domain]
TIGRFAMs	TIGR00558. pdxH. 1 hit.
PROSITE	PS01064. PYRIDOX_OXIDASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PDXH1_THICR

Accession

Primary (citable) accession number: Q31IR4

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 31, 2006
Last sequence update:	December 6, 2005
Last modified:	November 3, 2009
This is version 31 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)