Reviewed, UniProtKB/Swiss-Prot O61608 (NOS_ANOST)

Names and origin

Protein names	Recommended name:     Nitric oxide synthase       Short name=NOS     EC=1.14.13.39
Organism	Anopheles stephensi (Indo-Pakistan malaria mosquito)
Taxonomic identifier	30069 [NCBI]
Taxonomic lineage	Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Nematocera › Culicoidea › Culicidae › Anophelinae › Anopheles › stephensi species complex

Protein attributes

Sequence length	1247 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Produces nitric oxide (NO) which is a messenger molecule with diverse functions throughout the body. Nitric oxide limits plasmodium development in the midgut. Ref.1
Catalytic activity	L-arginine + n NADPH + n H+ + m O2 = citrulline + nitric oxide + n NADP+.
Cofactor	Heme group By similarity. Binds 1 FAD By similarity. Binds 1 FMN By similarity.
Enzyme regulation	Stimulated by calcium/calmodulin By similarity.
Induction	Detected in the midgut and carcass soon after invasion of the midgut by plasmodium. Early induction is also primed by bacterial growth in the blood meal. Ref.1
Sequence similarities	Belongs to the NOS family. Contains 1 FAD-binding FR-type domain. Contains 1 flavodoxin-like domain.

Ontologies

Keywords
Ligand	Calmodulin-binding FAD FMN Heme Iron Metal-binding NADP
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	nitric oxide biosynthetic process Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	FAD binding Inferred from electronic annotation. Source: InterPro FMN binding Inferred from electronic annotation. Source: InterPro NADP or NADPH binding Inferred from electronic annotation. Source: InterPro calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW heme binding Inferred from electronic annotation. Source: InterPro nitric-oxide synthase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1247	1247	Nitric oxide synthase		PRO_0000170950
Regions
	Domain	567 – 766	200	Flavodoxin-like
	Domain	795 – 1065	271	FAD-binding FR-type
	Nucleotide binding	712 – 743	32	FMN By similarity
	Nucleotide binding	855 – 866	12	FAD By similarity
	Nucleotide binding	998 – 1008	11	FAD By similarity
	Nucleotide binding	1073 – 1091	19	NADP By similarity
	Nucleotide binding	1170 – 1185	16	NADP By similarity
	Region	537 – 557	21	Calmodulin-binding Potential
	Compositional bias	51 – 54	4	Poly-Gly
Sites
	Metal binding	224	1	Iron (heme axial ligand) By similarity

Sequences

	Sequence		Length	Mass (Da)
	O61608-1 [UniParc]. Last modified January 1, 1999. Version 2. Checksum: 5F435E5EAC3D3778	FASTA	1,247	141,651
	10 20 30 40 50 60 MADTTTVVVE RREVAEGRES SKANHIGEER RGYDVSRKRC SISVHGGGTE GGGGNMRTNY 70 80 90 100 110 120 RELSPASLRI HRKSSHDIRN TLLGPDGEVL HLHDPSGKGG DGMGKMPAVV KPIKLKSIVT 130 140 150 160 170 180 KAESYDTMHG KASDVMSCSR EVCMGSVMTP HVIGTETRKP EIVQQHAKDF LDQYYSSIRR 190 200 210 220 230 240 LKSPAHDSRW QQVQKEVEAT GSYHLTETEL IYGAKLAWRN SSRCIGRIQW SKLQVFDCRY 250 260 270 280 290 300 VTTTSGMFEA ICNHIKYATN KGNLRSAITI FPQRTDGKHD YRIWNNQIIS YAGYKNADGK 310 320 330 340 350 360 IIGDPANVEF TDFCVKLGWK SKRTEWDILP LVVSANGHDP DYFDYPPELI LEVPLSHPQF 370 380 390 400 410 420 KWFAELNLRW YAVPMVSSML FDCGGIQFTA TAFSGWYMST EIGCRNLCDA NRRNLLEPIA 430 440 450 460 470 480 IKMGLDTRNP TSLWKDKALV EINIAVLHSY QSRNITIVDH HTASESFMKH FENETKLRNG 490 500 510 520 530 540 CPADWIWIVP PMSASVTPVF HQEMAVYYLR PSFEYQESAM KTHIWKKGRD SAKNKKPRRK 550 560 570 580 590 600 FNFKQIARAV KFTSKLFGRA LSRRIKATVL YATETGRSEQ YARQLVELLG HAFNAQIYCM 610 620 630 640 650 660 SDYDISSIEH EALLLVVAST FGNGDPPENG ELFAQDLYAM KLHESGHHQA HSELTIAASS 670 680 690 700 710 720 KSFIKANSRS DLGKFGPMGG RKIDRLDSLR GSTTDTLSEE TFGPLSNVRF AVFALGSSAY 730 740 750 760 770 780 PNFCAFGKYI DNILGELGGE RLMKMATGDE ICGQEQAFRK WAPEVFKIAC ETFCLDPEET 790 800 810 820 830 840 LSDAAFALQS ELSENTVRYA PVAEYESLDR ALSKFHNKKS MECSVKRNPI NLHCEMNGTE 850 860 870 880 890 900 RSTILVEIMA EGIDYEPGDH VGIFPANRKE IVDGIIERLT GVNDPDEMLQ LQVLKEKQTQ 910 920 930 940 950 960 NGVYKSWEPH ERLPVCTLRT LLTRFLDITT PPTRQLLTYL ASCCGDKADE ERLLMLANES 970 980 990 1000 1010 1020 SVYEDWRYWK LPHLLEVLEE FPSCRPPAAV FVAQLNALQP RFYSISSSPR KYSNEIHLTV 1030 1040 1050 1060 1070 1080 AIVTYRAEDG EGAEHYGVCS NYLANLQSDD KIYLFVRSAP SFHMSKDRTK PVILIGPGTG 1090 1100 1110 1120 1130 1140 IAPFRSFWQE WDHIKTEMVD CKIPKVWLFF GCRTKNVDLY RDEKEEMVQH GVLDRVFLAL 1150 1160 1170 1180 1190 1200 SREENIPKTY VQDLALKEAE SISELIMQEK GHIYVCGDVT MAEHVYQTLR KILATREKRT 1210 1220 1230 1240 ETEMEKYMLT LRDENRYHED IFGITLRTAE IHNKSRATAR IRMASQP

References

[1]	"The mosquito Anopheles stephensi limits malaria parasite development with inducible synthesis of nitric oxide." Luckhart S., Vodovotz Y., Cui L., Rosenberg R. Proc. Natl. Acad. Sci. U.S.A. 95:5700-5705(1998) [PubMed: 9576947] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, INDUCTION.
[2]	"Gene structure and polymorphism of an invertebrate nitric oxide synthase gene." Luckhart S., Rosenberg R. Gene 232:25-34(1999) [PubMed: 10333518] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF130134 , AF130124, AF130125, AF130126, AF130127, AF130128, AF130129, AF130130, AF130131, AF130132, AF130133 Genomic DNA. Translation: AAC68577.1.
PIR	T31331.
3D structure databases
SMR	O61608. Positions 113-525, 794-1224.
ModBase	Search...
Enzyme and pathway databases
BRENDA	1.14.13.39. 165156.
Family and domain databases
InterPro	IPR003097. FAD-binding_1. IPR017927. Fd_Rdtase_FAD-bd. IPR001094. Flavdoxin-like. IPR008254. Flavodoxin/NO_synth. IPR001709. Flavoprot_Pyr_Nucl_cyt_Rdtase. IPR012144. Nitric-oxide_synthase. IPR004030. NO_synthase_oxygenase_dom. IPR001433. OxRdtase_FAD/NAD_bd. IPR017938. Riboflavin_synthase-like_b-brl. [Graphical view]
Gene3D	G3DSA:3.90.340.10. NO_synthase_oxygenase_reg. 1 hit.
Pfam	PF00667. FAD_binding_1. 1 hit. PF00258. Flavodoxin_1. 1 hit. PF00175. NAD_binding_1. 1 hit. PF02898. NO_synthase. 1 hit. [Graphical view]
PIRSF	PIRSF000333. NOS. 1 hit.
PRINTS	PR00369. FLAVODOXIN. PR00371. FPNCR.
PROSITE	PS51384. FAD_FR. 1 hit. PS50902. FLAVODOXIN_LIKE. 1 hit. PS60001. NOS. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

NOS_ANOST

Accession

Primary (citable) accession number: O61608

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	January 1, 1999
Last modified:	January 19, 2010
This is version 72 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)